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Entry version 152 (13 Feb 2019)
Sequence version 2 (01 Dec 2000)
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Protein

Nucleic acid dioxygenase ALKBH1

Gene

ALKBH1

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

Dioxygenase that acts as on nucleic acids, such as DNA and tRNA (PubMed:18603530, PubMed:27745969, PubMed:27497299). Requires molecular oxygen, alpha-ketoglutarate and iron (PubMed:18603530, PubMed:27497299). A number of activities have been described for this dioxygenase, but recent results suggest that it mainly acts as on tRNAs and mediates their demethylation or oxidation depending on the context and subcellular compartment (PubMed:27745969, PubMed:27497299). Mainly acts as a tRNA demethylase by removing N1-methyladenine from various tRNAs, with a preference for N1-methyladenine at position 58 (m1A58) present on a stem loop structure of tRNAs (PubMed:27745969). Acts as a regulator of translation initiation and elongation in response to glucose deprivation: regulates both translation initiation, by mediating demethylation of tRNA(Met), and translation elongation, N1-methyladenine-containing tRNAs being preferentially recruited to polysomes to promote translation elongation (PubMed:27745969). In mitochondrion, specifically interacts with mt-tRNA(Met) and mediates oxidation of mt-tRNA(Met) methylated at cytosine(34) to form 5-formylcytosine (f5c) at this position (PubMed:27497299). mt-tRNA(Met) containing the f5c modification at the wobble position enables recognition of the AUA codon in addition to the AUG codon, expanding codon recognition in mitochondrial translation (PubMed:27497299). Specifically demethylates DNA methylated on the 6th position of adenine (N6-methyladenosine) DNA (PubMed:30017583). N6-methyladenosine (m6A) DNA is present at some L1 elements in embryonic stem cells and probably promotes their silencing (By similarity). Also able to repair alkylated single-stranded DNA and RNA containing 3-methylcytosine by oxidative demethylation, but with low activity (PubMed:18603530). Also has DNA lyase activity and introduces double-stranded breaks at abasic sites: cleaves both single-stranded DNA and double-stranded DNA at abasic sites, with the greatest activity towards double-stranded DNA with two abasic sites (PubMed:19959401). DNA lyase activity does not require alpha-ketboglutarate and iron and leads to the formation of an irreversible covalent protein-DNA adduct with the 5' DNA product (PubMed:19959401, PubMed:23577621). DNA lyase activity is not required during base excision repair and class switch recombination of the immunoglobulin heavy chain during B lymphocyte activation. May play a role in placental trophoblast lineage differentiation (By similarity).By similarity6 Publications

Caution

The DNA N6-methyl adenine demethylase activity is subject to discussion. According to a report, biochemical assays do not reveal clear DNA N6-methyl adenine demethylase activity in vivo (PubMed:27745969). According to another study, has clear DNA N6-methyl adenine demethylase activity (PubMed:30017583).2 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

  • The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.1 Publication EC:4.2.99.18

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Fe2+PROSITE-ProRule annotation2 PublicationsNote: Binds 1 Fe2+ ion per subunit.PROSITE-ProRule annotation

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>Sitei133Primary catalytic residue forming the imine linkage with DNA1 Publication1
Sitei133Secondary catalytic residue forming the imine linkage with DNA1 Publication1
<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 sitei144SubstrateBy similarity1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi231Iron; catalyticPROSITE-ProRule annotation2 Publications1
Metal bindingi233Iron; catalyticPROSITE-ProRule annotation3 Publications1
Binding sitei233SubstrateBy similarity1
Metal bindingi287Iron; catalyticPROSITE-ProRule annotation1

<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 functionDioxygenase, Lyase, Multifunctional enzyme, Oxidoreductase
Biological processDNA damage, DNA repair, RNA repair, Translation regulation
LigandIron, Metal-binding

<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:
Nucleic acid dioxygenase ALKBH1Curated (EC:1.14.11.-1 Publication)
Alternative name(s):
Alkylated DNA repair protein alkB homolog 11 Publication
Alpha-ketoglutarate-dependent dioxygenase ABH11 Publication
DNA 6mA demethylaseBy similarity
DNA N6-methyl adenine demethylaseCurated (EC:1.14.11.511 Publication)
DNA lyase ABH11 Publication (EC:4.2.99.181 Publication)
DNA oxidative demethylase ALKBH1 (EC:1.14.11.331 Publication)
tRNA N1-methyl adenine demethylase1 Publication (EC:1.14.11.-1 Publication)
<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:ALKBH1Imported
Synonyms:ABH1 Publication, ABH11 Publication, ALKBH
<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 14

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000100601.9

Human Gene Nomenclature Database

More...
HGNCi
HGNC:17911 ALKBH1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
605345 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q13686

<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

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

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>Mutagenesisi3K → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi25K → A: Moderate decrease in DNA lyase activity. Reduced DNA lyase activity; when associated with A-133. 1 Publication1
Mutagenesisi55K → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi61K → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi64K → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi87K → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi94K → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi113H → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi116K → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi118C → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi120K → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi125K → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi129C → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi133K → A: Reduced DNA lyase activity. Slightly more reduced DNA lyase activity; when associated with A-25. Strongly reduced activity; when associated with A-154. 1 Publication1
Mutagenesisi134H → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi137K → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi148K → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi154K → A: Does not affect DNA lyase activity. Strongly reduced activity; when associated with A-133. 1 Publication1
Mutagenesisi158K → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi167K → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi182K → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi183K → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi218I → L: Reduces Fe2OG dioxygenase activity by 50%. 1 Publication1
Mutagenesisi231 – 233HVD → AVA: Loss of catalytic activity. Abolishes ability to regulate translation in respose to glucose deprivation. 1 Publication3
Mutagenesisi231H → A: Near loss of Fe2OG dioxygenase activity. No effect on DNA lyase activity. 2 Publications1
Mutagenesisi233D → A: Loss of Fe2OG dioxygenase activity. No effect on DNA lyase activity. Abolishes ability to mediate oxidation of mt-tRNA(Met) methylated at cytosine(34) to form 5-formylcytosine (f(5)c). Abolished DNA N6-methyl adenine demethylase activity. 4 Publications1
Mutagenesisi241K → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi287H → A: Loss of Fe2OG dioxygenase activity. No effect on DNA lyase activity. 2 Publications1
Mutagenesisi303H → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi304C → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi335K → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi338R → A: Reduced Fe2OG dioxygenase activity. Abolishes ability to mediate oxidation of mt-tRNA(Met) methylated at cytosine(34) to form 5-formylcytosine (f(5)c). 2 Publications1
Mutagenesisi344R → A: Reduced Fe2OG dioxygenase activity. 1 Publication1
Mutagenesisi362K → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi371C → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi372H → A: Does not affect DNA lyase activity. 1 Publication1
Mutagenesisi381K → A: Does not affect DNA lyase activity. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
8846

Open Targets

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OpenTargetsi
ENSG00000100601

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA134906996

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ALKBH1

<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_00000666681 – 389Nucleic acid dioxygenase ALKBH1Add BLAST389

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q13686

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q13686

MaxQB - The MaxQuant DataBase

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MaxQBi
Q13686

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

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PaxDbi
Q13686

PeptideAtlas

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PeptideAtlasi
Q13686

PRoteomics IDEntifications database

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PRIDEi
Q13686

ProteomicsDB human proteome resource

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ProteomicsDBi
59661

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q13686

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

More...
PhosphoSitePlusi
Q13686

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitous.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000100601 Expressed in 211 organ(s), highest expression level in oocyte

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q13686 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q13686 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA044087

<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

Monomer (PubMed:19959401). Interacts with DNAJB6 (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
114372, 2 interactors

Protein interaction database and analysis system

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IntActi
Q13686, 1 interactor

STRING: functional protein association networks

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STRINGi
9606.ENSP00000216489

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q13686

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini208 – 347Fe2OG dioxygenasePROSITE-ProRule annotationAdd BLAST140

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>Regioni86 – 389tRNA-binding1 PublicationAdd BLAST304
Regioni175 – 177Substrate bindingBy similarity3
Regioni220 – 222Alpha-ketoglutarate bindingBy similarity3
Regioni338 – 344Alpha-ketoglutarate bindingBy similarity7

<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 alkB family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2731 Eukaryota
COG3145 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000004599

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000033905

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG050487

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q13686

KEGG Orthology (KO)

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KOi
K10765

Identification of Orthologs from Complete Genome Data

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OMAi
CGFQGFR

Database of Orthologous Groups

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OrthoDBi
1045321at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q13686

TreeFam database of animal gene trees

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TreeFami
TF314609

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.120.590, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR004574 Alkb
IPR027450 AlkB-like
IPR037151 AlkB-like_sf
IPR005123 Oxoglu/Fe-dep_dioxygenase

The PANTHER Classification System

More...
PANTHERi
PTHR16557 PTHR16557, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF13532 2OG-FeII_Oxy_2, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00568 alkb, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51471 FE2OG_OXY, 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

Q13686-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGKMAAAVGS VATLATEPGE DAFRKLFRFY RQSRPGTADL EGVIDFSAAH
60 70 80 90 100
AARGKGPGAQ KVIKSQLNVS SVSEQNAYRA GLQPVSKWQA YGLKGYPGFI
110 120 130 140 150
FIPNPFLPGY QWHWVKQCLK LYSQKPNVCN LDKHMSKEET QDLWEQSKEF
160 170 180 190 200
LRYKEATKRR PRSLLEKLRW VTVGYHYNWD SKKYSADHYT PFPSDLGFLS
210 220 230 240 250
EQVAAACGFE DFRAEAGILN YYRLDSTLGI HVDRSELDHS KPLLSFSFGQ
260 270 280 290 300
SAIFLLGGLQ RDEAPTAMFM HSGDIMIMSG FSRLLNHAVP RVLPNPEGEG
310 320 330 340 350
LPHCLEAPLP AVLPRDSMVE PCSMEDWQVC ASYLKTARVN MTVRQVLATD
360 370 380
QNFPLEPIED EKRDISTEGF CHLDDQNSEV KRARINPDS
Length:389
Mass (Da):43,832
Last modified:December 1, 2000 - 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:i539C4CE41D2D8AEC
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
G3V4M4G3V4M4_HUMAN
Nucleic acid dioxygenase ALKBH1
ALKBH1
116Annotation 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>
H0YJF3H0YJF3_HUMAN
Nucleic acid dioxygenase ALKBH1
ALKBH1
112Annotation 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 CAA63047 differs from that shown. Reason: Frameshift at several positions.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 conflicti133K → T in CAA63047 (PubMed:8600462).Curated1
Sequence conflicti266 – 267TA → PP in CAA63047 (PubMed:8600462).Curated2
Sequence conflicti388D → H in AAH25787 (PubMed:15489334).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_048221135M → I. Corresponds to variant dbSNP:rs17825440Ensembl.1
Natural variantiVAR_048222324M → L. Corresponds to variant dbSNP:rs6494Ensembl.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
X91992 mRNA Translation: CAA63047.1 Frameshift.
AC008044 Genomic DNA Translation: AAF01478.1
BC025787 mRNA Translation: AAH25787.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS32127.1

Protein sequence database of the Protein Information Resource

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PIRi
S64736

NCBI Reference Sequences

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RefSeqi
NP_006011.2, NM_006020.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.94542

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000216489; ENSP00000216489; ENSG00000100601

Database of genes from NCBI RefSeq genomes

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GeneIDi
8846

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:8846

UCSC genome browser

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UCSCi
uc001xuc.2 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91992 mRNA Translation: CAA63047.1 Frameshift.
AC008044 Genomic DNA Translation: AAF01478.1
BC025787 mRNA Translation: AAH25787.1
CCDSiCCDS32127.1
PIRiS64736
RefSeqiNP_006011.2, NM_006020.2
UniGeneiHs.94542

3D structure databases

ProteinModelPortaliQ13686
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114372, 2 interactors
IntActiQ13686, 1 interactor
STRINGi9606.ENSP00000216489

PTM databases

iPTMnetiQ13686
PhosphoSitePlusiQ13686

Polymorphism and mutation databases

BioMutaiALKBH1

Proteomic databases

EPDiQ13686
jPOSTiQ13686
MaxQBiQ13686
PaxDbiQ13686
PeptideAtlasiQ13686
PRIDEiQ13686
ProteomicsDBi59661

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
8846
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216489; ENSP00000216489; ENSG00000100601
GeneIDi8846
KEGGihsa:8846
UCSCiuc001xuc.2 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
8846
DisGeNETi8846
EuPathDBiHostDB:ENSG00000100601.9

GeneCards: human genes, protein and diseases

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GeneCardsi
ALKBH1

H-Invitational Database, human transcriptome db

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H-InvDBi
HIX0011855
HGNCiHGNC:17911 ALKBH1
HPAiHPA044087
MIMi605345 gene
neXtProtiNX_Q13686
OpenTargetsiENSG00000100601
PharmGKBiPA134906996

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2731 Eukaryota
COG3145 LUCA
GeneTreeiENSGT00390000004599
HOGENOMiHOG000033905
HOVERGENiHBG050487
InParanoidiQ13686
KOiK10765
OMAiCGFQGFR
OrthoDBi1045321at2759
PhylomeDBiQ13686
TreeFamiTF314609

Miscellaneous databases

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

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ChiTaRSi
ALKBH1 human

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

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GenomeRNAii
8846

Protein Ontology

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PROi
PR:Q13686

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000100601 Expressed in 211 organ(s), highest expression level in oocyte
ExpressionAtlasiQ13686 baseline and differential
GenevisibleiQ13686 HS

Family and domain databases

Gene3Di2.60.120.590, 1 hit
InterProiView protein in InterPro
IPR004574 Alkb
IPR027450 AlkB-like
IPR037151 AlkB-like_sf
IPR005123 Oxoglu/Fe-dep_dioxygenase
PANTHERiPTHR16557 PTHR16557, 1 hit
PfamiView protein in Pfam
PF13532 2OG-FeII_Oxy_2, 1 hit
TIGRFAMsiTIGR00568 alkb, 1 hit
PROSITEiView protein in PROSITE
PS51471 FE2OG_OXY, 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 nameiALKB1_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: Q13686
Secondary accession number(s): Q8TAU1, Q9ULA7
<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: December 1, 2000
Last sequence update: December 1, 2000
Last modified: February 13, 2019
This is version 152 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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