Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P49789 (FHIT_HUMAN)

Protein

Bis(5'-adenosyl)-triphosphatase

Gene

FHIT

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

Cleaves P1-P3-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P1-P4-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P1-P3-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity, it may in part come from the mitochondrial form, which sensitizes the low-affinity Ca2+ transporters, enhancing mitochondrial calcium uptake. Functions as tumor suppressor.7 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei8SubstrateCombined sources1 Publication1
Binding sitei27SubstrateCombined sources1 Publication1
Binding sitei83SubstrateCombined sources1 Publication1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei96Tele-AMP-histidine intermediate2 Publications1
Binding sitei98SubstrateCombined sources1 Publication1
<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>Sitei114Important for induction of apoptosis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi89 – 92SubstrateCombined sources1 Publication4

<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

  • bis(5'-adenosyl)-triphosphatase activity Source: UniProtKB
  • catalytic activity Source: ProtInc
  • hydrolase activity Source: UniProtKB
  • identical protein binding Source: IntAct
  • nucleotide binding Source: UniProtKB-KW
  • ubiquitin protein ligase binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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

Molecular functionHydrolase
Biological processApoptosis, Transcription, Transcription regulation
LigandManganese, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.6.1.29 2681

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P49789

SIGNOR Signaling Network Open Resource

More...SIGNORi		P49789

<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:
Bis(5'-adenosyl)-triphosphatase (EC:3.6.1.29)
Alternative name(s):
AP3A hydrolase
Short name:
AP3Aase
Diadenosine 5',5'''-P1,P3-triphosphate hydrolase
Dinucleosidetriphosphatase
Fragile histidine triad protein
<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:FHIT
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000189283.9

Human Gene Nomenclature Database

More...HGNCi		HGNC:3701 FHIT

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601153 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P49789

<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

Cytoplasm, Mitochondrion, Nucleus

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

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

A chromosomal aberration involving FHIT has been found in a lymphoblastoid cell line established from a family with renal cell carcinoma and thyroid carcinoma. Translocation t(3;8)(p14.2;q24.1) with RNF139. Although the 3p14.2 breakpoint has been shown to interrupt FHIT in its 5-prime non-coding region, it is unlikely that FHIT is causally related to renal or other malignancies.1 Publication
Associated with digestive tract cancers. Numerous tumor types are found to have aberrant forms of FHIT protein due to deletions in a coding region of chromosome 3p14.2 including the fragile site locus FRA3B.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>Mutagenesisi10I → W: Strongly reduces affinity for substrates and impairs apoptosis; when associated with W-25. 1 Publication1
Mutagenesisi25L → W: Reduces affinity for substrates and impairs apoptosis. Strongly reduces affinity for substrates and impairs apoptosis; when associated with W-10. 1 Publication1
Mutagenesisi35H → N: 50% decrease in catalytic activity. No loss in substrate binding. 1 Publication1
Mutagenesisi94H → N: 75% decrease in catalytic activity. No loss in substrate binding. 1 Publication1
Mutagenesisi96H → D: Loss of catalytic activity. 4 Publications1
Mutagenesisi96H → G: Total loss of catalytic activity. Rescuable with free imidazole. 4 Publications1
Mutagenesisi96H → N: Total loss of catalytic activity. No loss in substrate binding. 4 Publications1
Mutagenesisi98H → N: 98% decrease in catalytic activity. 1 Publication1
Mutagenesisi114Y → A: Impairs induction of apoptosis. Strongly reduced affinity for substrates. 2 Publications1
Mutagenesisi114Y → D: Impairs induction of apoptosis. Reduces affinity for substrates. 2 Publications1
Mutagenesisi114Y → F: Loss of phosphorylation by SRC. Impairs induction of apoptosis. 2 Publications1
Mutagenesisi145Y → F: No effect on phosphorylation by SRC. 1 Publication1

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNET

More...DisGeNETi		2272

MalaCards human disease database

More...MalaCardsi		FHIT

Open Targets

More...OpenTargetsi		ENSG00000189283

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

More...Orphaneti		422526 Hereditary clear cell renal cell carcinoma

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA28140

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1795151

Drug and drug target database

More...DrugBanki		DB02373 Adenosine Monotungstate
DB04389 Ado-P-Ch2-P-Ps-Ado
DB04173 Fructose

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		FHIT

Domain mapping of disease mutations (DMDM)

More...DMDMi		1706794

<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_00001097891 – 147Bis(5'-adenosyl)-triphosphataseAdd BLAST147

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 residuei114Phosphotyrosine; by SRC1 Publication1
Modified residuei145Phosphotyrosine1 Publication1

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

Phosphorylation at Tyr-114 by SRC is required for induction of apoptosis.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P49789

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

More...PaxDbi		P49789

PeptideAtlas

More...PeptideAtlasi		P49789

PRoteomics IDEntifications database

More...PRIDEi		P49789

ProteomicsDB human proteome resource

More...ProteomicsDBi		56119

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P49789

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

More...PhosphoSitePlusi		P49789

<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

Low levels expressed in all tissues tested. Phospho-FHIT observed in liver and kidney, but not in brain and lung. Phospho-FHIT undetected in all tested human tumor cell lines.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000189283 Expressed in 131 organ(s), highest expression level in pigmented layer of retina

CleanEx database of gene expression profiles

More...CleanExi		HS_FHIT

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P49789 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P49789 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB002684
HPA018840
HPA018909

<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. Interacts with UBE2I. Interacts with MDM2. Interacts with CTNNB1. Identified in a complex with CTNNB1 and LEF1.6 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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108563, 14 interactors

Database of interacting proteins

More...DIPi		DIP-29947N

Protein interaction database and analysis system

More...IntActi		P49789, 5 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000342087

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P49789

<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

1147
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P49789

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

More...SMRi		P49789

Database of comparative protein structure models

More...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		P49789

<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>Domaini2 – 109HITPROSITE-ProRule annotationAdd BLAST108

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>Motifi94 – 98Histidine triad motifPROSITE-ProRule annotation5

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3379 Eukaryota
COG0537 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00510000047967

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000164170

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG051614

KEGG Orthology (KO)

More...KOi		K01522

Identification of Orthologs from Complete Genome Data

More...OMAi		IIPRKKA

Database of Orthologous Groups

More...OrthoDBi		EOG091G0RR0

Database for complete collections of gene phylogenies

More...PhylomeDBi		P49789

TreeFam database of animal gene trees

More...TreeFami		TF105432

Family and domain databases

Conserved Domains Database

More...CDDi		cd01275 FHIT, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.428.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR039383 FHIT
IPR019808 Histidine_triad_CS
IPR001310 Histidine_triad_HIT
IPR011146 HIT-like
IPR036265 HIT-like_sf

The PANTHER Classification System

More...PANTHERi		PTHR23089 PTHR23089, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01230 HIT, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF54197 SSF54197, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00892 HIT_1, 1 hit
PS51084 HIT_2, 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 2 potential isoforms that are computationally mapped.Show allAlign All

P49789-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSFRFGQHLI KPSVVFLKTE LSFALVNRKP VVPGHVLVCP LRPVERFHDL 
        60         70         80         90        100
RPDEVADLFQ TTQRVGTVVE KHFHGTSLTF SMQDGPEAGQ TVKHVHVHVL 
       110        120        130        140 
PRKAGDFHRN DSIYEELQKH DKEDFPASWR SEEEMAAEAA ALRVYFQ
Length:147
Mass (Da):16,858
Last modified:January 23, 2007 - v3
<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:i14D85961A19ECF3E
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
E9PBZ0E9PBZ0_HUMAN
Bis(5'-adenosyl)-triphosphatase
FHIT
78Annotation 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>
A0A0A0MRB0A0A0A0MRB0_HUMAN
Bis(5'-adenosyl)-triphosphatase
FHIT
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>

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 conflicti146F → S in BAF82513 (PubMed:14702039).Curated1

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 16733 Da from positions 2 - 147. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
U46922 mRNA Translation: AAA99013.1
U76271
, U76267, U76268, U76269, U76270 Genomic DNA Translation: AAB52539.1
KJ534835 mRNA Translation: AHW56475.1
AY625256 Genomic DNA Translation: AAT37530.1
DQ120721 mRNA Translation: AAZ23623.1
EF186677 Genomic DNA Translation: ABM65879.1
EF183457 Genomic DNA Translation: ABM66086.1
EF183458 Genomic DNA Translation: ABM66087.1
EF183459 Genomic DNA Translation: ABM66088.1
EF183461 Genomic DNA Translation: ABM66090.1
EF183464 Genomic DNA Translation: ABM66093.1
AK289824 mRNA Translation: BAF82513.1
CH471055 Genomic DNA Translation: EAW65393.1
BC032336 mRNA Translation: AAH32336.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS2894.1

Protein sequence database of the Protein Information Resource

More...PIRi		A58802

NCBI Reference Sequences

More...RefSeqi		NP_001159715.1, NM_001166243.2
NP_001307828.1, NM_001320899.1
NP_001307829.1, NM_001320900.1
NP_002003.1, NM_002012.3

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.655995

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000468189; ENSP00000417480; ENSG00000189283
ENST00000476844; ENSP00000417557; ENSG00000189283
ENST00000492590; ENSP00000418582; ENSG00000189283

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2272

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2272

UCSC genome browser

More...UCSCi		uc003dkx.5 human

Keywords - Coding sequence diversityi

Chromosomal rearrangement

<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
U46922 mRNA Translation: AAA99013.1
U76271
, U76267, U76268, U76269, U76270 Genomic DNA Translation: AAB52539.1
KJ534835 mRNA Translation: AHW56475.1
AY625256 Genomic DNA Translation: AAT37530.1
DQ120721 mRNA Translation: AAZ23623.1
EF186677 Genomic DNA Translation: ABM65879.1
EF183457 Genomic DNA Translation: ABM66086.1
EF183458 Genomic DNA Translation: ABM66087.1
EF183459 Genomic DNA Translation: ABM66088.1
EF183461 Genomic DNA Translation: ABM66090.1
EF183464 Genomic DNA Translation: ABM66093.1
AK289824 mRNA Translation: BAF82513.1
CH471055 Genomic DNA Translation: EAW65393.1
BC032336 mRNA Translation: AAH32336.1
CCDSiCCDS2894.1
PIRiA58802
RefSeqiNP_001159715.1, NM_001166243.2
NP_001307828.1, NM_001320899.1
NP_001307829.1, NM_001320900.1
NP_002003.1, NM_002012.3
UniGeneiHs.655995

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FHIX-ray3.10A1-147[»]
1FITX-ray1.85A1-147[»]
2FHIX-ray2.60A1-147[»]
2FITX-ray1.90A1-147[»]
3FITX-ray2.40A1-147[»]
4FITX-ray2.50A1-147[»]
5FITX-ray2.30A1-147[»]
6FITX-ray2.60A1-147[»]
ProteinModelPortaliP49789
SMRiP49789
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108563, 14 interactors
DIPiDIP-29947N
IntActiP49789, 5 interactors
STRINGi9606.ENSP00000342087

Chemistry databases

BindingDBiP49789
ChEMBLiCHEMBL1795151
DrugBankiDB02373 Adenosine Monotungstate
DB04389 Ado-P-Ch2-P-Ps-Ado
DB04173 Fructose

PTM databases

iPTMnetiP49789
PhosphoSitePlusiP49789

Polymorphism and mutation databases

BioMutaiFHIT
DMDMi1706794

Proteomic databases

EPDiP49789
PaxDbiP49789
PeptideAtlasiP49789
PRIDEiP49789
ProteomicsDBi56119

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		2272
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000468189; ENSP00000417480; ENSG00000189283
ENST00000476844; ENSP00000417557; ENSG00000189283
ENST00000492590; ENSP00000418582; ENSG00000189283
GeneIDi2272
KEGGihsa:2272
UCSCiuc003dkx.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2272
DisGeNETi2272
EuPathDBiHostDB:ENSG00000189283.9

GeneCards: human genes, protein and diseases

More...GeneCardsi		FHIT
HGNCiHGNC:3701 FHIT
HPAiCAB002684
HPA018840
HPA018909
MalaCardsiFHIT
MIMi601153 gene
neXtProtiNX_P49789
OpenTargetsiENSG00000189283
Orphaneti422526 Hereditary clear cell renal cell carcinoma
PharmGKBiPA28140

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3379 Eukaryota
COG0537 LUCA
GeneTreeiENSGT00510000047967
HOGENOMiHOG000164170
HOVERGENiHBG051614
KOiK01522
OMAiIIPRKKA
OrthoDBiEOG091G0RR0
PhylomeDBiP49789
TreeFamiTF105432

Enzyme and pathway databases

BRENDAi3.6.1.29 2681
SABIO-RKiP49789
SIGNORiP49789

Miscellaneous databases

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

More...ChiTaRSi		FHIT human
EvolutionaryTraceiP49789

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		FHIT

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

More...GenomeRNAii		2272

Protein Ontology

More...PROi		PR:P49789

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000189283 Expressed in 131 organ(s), highest expression level in pigmented layer of retina
CleanExiHS_FHIT
ExpressionAtlasiP49789 baseline and differential
GenevisibleiP49789 HS

Family and domain databases

CDDicd01275 FHIT, 1 hit
Gene3Di3.30.428.10, 1 hit
InterProiView protein in InterPro
IPR039383 FHIT
IPR019808 Histidine_triad_CS
IPR001310 Histidine_triad_HIT
IPR011146 HIT-like
IPR036265 HIT-like_sf
PANTHERiPTHR23089 PTHR23089, 1 hit
PfamiView protein in Pfam
PF01230 HIT, 1 hit
SUPFAMiSSF54197 SSF54197, 1 hit
PROSITEiView protein in PROSITE
PS00892 HIT_1, 1 hit
PS51084 HIT_2, 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 nameiFHIT_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: P49789
Secondary accession number(s): A2IAS9
, A2IAT0, A2IAT6, A8K1A9, Q45QG9, Q6IU12
<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: October 1, 1996
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 172 of the entry and version 3 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. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again