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Entry version 206 (29 Sep 2021)
Sequence version 3 (25 Nov 2008)
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Protein

Lysine-specific demethylase 5A

Gene

KDM5A

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

Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Regulates specific gene transcription through DNA-binding on 5'-CCGCCC-3' motif (PubMed:18270511).

May stimulate transcription mediated by nuclear receptors. Involved in transcriptional regulation of Hox proteins during cell differentiation (PubMed:19430464).

May participate in transcriptional repression of cytokines such as CXCL12. Plays a role in the regulation of the circadian rhythm and in maintaining the normal periodicity of the circadian clock. In a histone demethylase-independent manner, acts as a coactivator of the CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER1/2 and other clock-controlled genes and increases histone acetylation at PER1/2 promoters by inhibiting the activity of HDAC1 (By similarity).

Seems to act as a transcriptional corepressor for some genes such as MT1F and to favor the proliferation of cancer cells (PubMed:27427228).

By similarity8 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

<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+By similarityNote: Binds 1 Fe2+ ion per subunit.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The inhibitors KDOAM-25, CPI-455 and others inhibits its demethylase activity, resulting to cell growth arrest in cancer cells.2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat are 2.1 min(-1) and 1.9 min(-1) for 2-oxoglutarate and histone H3K4me3, respectively.1 Publication
  1. KM=9 µM for 2-oxoglutarate1 Publication
  2. KM=2.9 µM for histone H3K4me31 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei4092-oxoglutarate2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi483Iron; catalyticPROSITE-ProRule annotation4 Publications1
Metal bindingi485Iron; catalytic4 Publications1
Binding sitei4912-oxoglutarate2 Publications1
Binding sitei4932-oxoglutarate2 Publications1
Binding sitei5012-oxoglutarate2 Publications1
Metal bindingi571Iron; catalyticPROSITE-ProRule annotation4 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri293 – 343PHD-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri676 – 728C5HC2Combined sources2 PublicationsAdd BLAST53
Zinc fingeri1161 – 1218PHD-type 2PROSITE-ProRule annotationAdd BLAST58
Zinc fingeri1607 – 1661PHD-type 31 PublicationAdd BLAST55

<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 functionActivator, Chromatin regulator, Developmental protein, Dioxygenase, Oxidoreductase
Biological processBiological rhythms, Transcription, Transcription regulation
LigandIron, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:ENSG00000073614-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.14.11.67, 2681

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
P29375

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-3214842, HDMs demethylate histones

SIGNOR Signaling Network Open Resource

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SIGNORi
P29375

<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:
Lysine-specific demethylase 5A (EC:1.14.11.673 Publications)
Alternative name(s):
Histone demethylase JARID1A
Jumonji/ARID domain-containing protein 1A
Retinoblastoma-binding protein 2
Short name:
RBBP-2
[histone H3]-trimethyl-L-lysine(4) demethylase 5ACurated
<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:KDM5AImported
Synonyms:JARID1A, RBBP2, RBP21 Publication
<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 12

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:9886, KDM5A

Online Mendelian Inheritance in Man (OMIM)

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MIMi
180202, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P29375

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSG00000073614

<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

Keywords - Cellular componenti

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 KDM5A has been found in M5 type acute myeloid leukemia. Translocation t(11;12)(p15;p13) with NUP98.1 Publication
Chromosomal aberrations involving KDM5A have been found in M7 type childhood acute myeloid leukemia. Translocation t(11;12)(p15;p13) with NUP98.2 Publications

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>Mutagenesisi112R → E: Decreases DNA-binding. 1 Publication1
Mutagenesisi152K → E: Abolishes DNA-binding. 1 Publication1
Mutagenesisi156S → D: Decreases DNA-binding. 1 Publication1
Mutagenesisi157L → E: Decreases DNA-binding. 1 Publication1
Mutagenesisi626C → S: No effect on lysine-specific histone demethylase activity; when associated with S-636. 1 Publication1
Mutagenesisi636C → S: No effect on lysine-specific histone demethylase activity; when associated with S-626. 1 Publication1
Mutagenesisi1609V → G: No effect on interaction with histone H3 di- and trimethylated at 'Lys-4'. 1 Publication1
Mutagenesisi1625W → A: Abolishes interaction with histone H3 di- and trimethylated at 'Lys-4'. 1 Publication1
Mutagenesisi1634 – 1635EW → AA: Abolishes interaction with histone H3 di- and trimethylated at 'Lys-4'. 1 Publication2

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>Sitei1485 – 1486Breakpoint for translocation to form the NUP98-KDM5A fusion protein1 Publication2

Organism-specific databases

DisGeNET

More...
DisGeNETi
5927

Open Targets

More...
OpenTargetsi
ENSG00000073614

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA34250

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
P29375, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2424504

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
2680

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
KDM5A

Domain mapping of disease mutations (DMDM)

More...
DMDMi
215274124

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002005841 – 1690Lysine-specific demethylase 5AAdd BLAST1690

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
<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 residuei204PhosphoserineCombined sources1
Cross-linki1007Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1111PhosphoserineCombined sources1
Modified residuei1330PhosphoserineCombined sources1
Modified residuei1331PhosphoserineCombined sources1
Modified residuei1343PhosphothreonineBy similarity1
Modified residuei1345PhosphoserineBy similarity1
Modified residuei1438PhosphoserineCombined sources1
Modified residuei1488PhosphoserineCombined sources1
Modified residuei1595PhosphotyrosineBy similarity1
Modified residuei1598PhosphoserineCombined sources1
Modified residuei1603PhosphoserineCombined sources1
Modified residuei1666PhosphoserineCombined sources1

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P29375

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P29375

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
P29375

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P29375

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

More...
PaxDbi
P29375

PeptideAtlas

More...
PeptideAtlasi
P29375

PRoteomics IDEntifications database

More...
PRIDEi
P29375

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
54559 [P29375-1]
54560 [P29375-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P29375

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

More...
PhosphoSitePlusi
P29375

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P29375

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000073614, Expressed in peritoneum and 254 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P29375, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P29375, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000073614, Low tissue specificity

<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 with SUZ12; the interaction is direct (By similarity).

Interacts with the viral protein-binding domain of RB1.

Interacts with ESR1, MYC, MYCN and LMO2.

Interacts with HDAC1 (By similarity).

Interacts with ARNTL/BMAL1 and CLOCK.

Interacts (via PHD-type 1 zinc finger) with histone H3 unmodified at 'Lys-4' and (via PHD-type 3 zinc finger) with histone H3 di- and trimethylated at 'Lys-4' (PubMed:19430464).

By similarity8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<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
111862, 50 interactors

Database of interacting proteins

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DIPi
DIP-472N

Protein interaction database and analysis system

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IntActi
P29375, 23 interactors

Molecular INTeraction database

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MINTi
P29375

STRING: functional protein association networks

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STRINGi
9606.ENSP00000382688

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P29375

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P29375, protein

<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

11690
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
P29375

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

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SMRi
P29375

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P29375

<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>Domaini19 – 60JmjNPROSITE-ProRule annotationAdd BLAST42
Domaini84 – 174ARIDPROSITE-ProRule annotationAdd BLAST91
Domaini437 – 603JmjCPROSITE-ProRule annotationAdd BLAST167

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>Regioni1327 – 1348DisorderedSequence analysisAdd BLAST22
Regioni1407 – 1433DisorderedSequence analysisAdd BLAST27
Regioni1490 – 1509DisorderedSequence analysisAdd BLAST20
Regioni1516 – 1543DisorderedSequence analysisAdd BLAST28
Regioni1623 – 1690Interaction with LMO21 PublicationAdd BLAST68

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>Motifi419 – 423GSGFP motifBy similarity5

<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 GSGFP motif is required for the interaction with SUZ12 (By similarity). The ARID domain specifically binds to the CCGCCC motif and is required for the lysine-specific histone demethylase activity (PubMed:18270511). The PHD-type 3 zinc finger is required for the interaction with histone H3 di- and trimethylated at 'Lys-4' (PubMed:19430464).By similarity2 Publications

<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 JARID1 histone demethylase family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri293 – 343PHD-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri676 – 728C5HC2Combined sources2 PublicationsAdd BLAST53
Zinc fingeri1161 – 1218PHD-type 2PROSITE-ProRule annotationAdd BLAST58
Zinc fingeri1607 – 1661PHD-type 31 PublicationAdd BLAST55

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1246, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000157170

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_000991_2_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P29375

Identification of Orthologs from Complete Genome Data

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OMAi
KWAPVAP

Database of Orthologous Groups

More...
OrthoDBi
664180at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P29375

TreeFam database of animal gene trees

More...
TreeFami
TF106476

Family and domain databases

Database of protein disorder

More...
DisProti
DP02224

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.150.60, 1 hit
3.30.40.10, 3 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001606, ARID_dom
IPR036431, ARID_dom_sf
IPR003347, JmjC_dom
IPR003349, JmjN
IPR013637, Lys_sp_deMease-like_dom
IPR019786, Zinc_finger_PHD-type_CS
IPR004198, Znf_C5HC2
IPR011011, Znf_FYVE_PHD
IPR001965, Znf_PHD
IPR019787, Znf_PHD-finger
IPR013083, Znf_RING/FYVE/PHD

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01388, ARID, 1 hit
PF02373, JmjC, 1 hit
PF02375, JmjN, 1 hit
PF00628, PHD, 2 hits
PF08429, PLU-1, 1 hit
PF02928, zf-C5HC2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00501, BRIGHT, 1 hit
SM00558, JmjC, 1 hit
SM00545, JmjN, 1 hit
SM00249, PHD, 3 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF46774, SSF46774, 1 hit
SSF57903, SSF57903, 3 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51011, ARID, 1 hit
PS51184, JMJC, 1 hit
PS51183, JMJN, 1 hit
PS01359, ZF_PHD_1, 2 hits
PS50016, ZF_PHD_2, 3 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)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 2 <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 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P29375-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MAGVGPGGYA AEFVPPPECP VFEPSWEEFT DPLSFIGRIR PLAEKTGICK
60 70 80 90 100
IRPPKDWQPP FACEVKSFRF TPRVQRLNEL EAMTRVRLDF LDQLAKFWEL
110 120 130 140 150
QGSTLKIPVV ERKILDLYAL SKIVASKGGF EMVTKEKKWS KVGSRLGYLP
160 170 180 190 200
GKGTGSLLKS HYERILYPYE LFQSGVSLMG VQMPNLDLKE KVEPEVLSTD
210 220 230 240 250
TQTSPEPGTR MNILPKRTRR VKTQSESGDV SRNTELKKLQ IFGAGPKVVG
260 270 280 290 300
LAMGTKDKED EVTRRRKVTN RSDAFNMQMR QRKGTLSVNF VDLYVCMFCG
310 320 330 340 350
RGNNEDKLLL CDGCDDSYHT FCLIPPLPDV PKGDWRCPKC VAEECSKPRE
360 370 380 390 400
AFGFEQAVRE YTLQSFGEMA DNFKSDYFNM PVHMVPTELV EKEFWRLVSS
410 420 430 440 450
IEEDVIVEYG ADISSKDFGS GFPVKDGRRK ILPEEEEYAL SGWNLNNMPV
460 470 480 490 500
LEQSVLAHIN VDISGMKVPW LYVGMCFSSF CWHIEDHWSY SINYLHWGEP
510 520 530 540 550
KTWYGVPSHA AEQLEEVMRE LAPELFESQP DLLHQLVTIM NPNVLMEHGV
560 570 580 590 600
PVYRTNQCAG EFVVTFPRAY HSGFNQGYNF AEAVNFCTAD WLPIGRQCVN
610 620 630 640 650
HYRRLRRHCV FSHEELIFKM AADPECLDVG LAAMVCKELT LMTEEETRLR
660 670 680 690 700
ESVVQMGVLM SEEEVFELVP DDERQCSACR TTCFLSALTC SCNPERLVCL
710 720 730 740 750
YHPTDLCPCP MQKKCLRYRY PLEDLPSLLY GVKVRAQSYD TWVSRVTEAL
760 770 780 790 800
SANFNHKKDL IELRVMLEDA EDRKYPENDL FRKLRDAVKE AETCASVAQL
810 820 830 840 850
LLSKKQKHRQ SPDSGRTRTK LTVEELKAFV QQLFSLPCVI SQARQVKNLL
860 870 880 890 900
DDVEEFHERA QEAMMDETPD SSKLQMLIDM GSSLYVELPE LPRLKQELQQ
910 920 930 940 950
ARWLDEVRLT LSDPQQVTLD VMKKLIDSGV GLAPHHAVEK AMAELQELLT
960 970 980 990 1000
VSERWEEKAK VCLQARPRHS VASLESIVNE AKNIPAFLPN VLSLKEALQK
1010 1020 1030 1040 1050
AREWTAKVEA IQSGSNYAYL EQLESLSAKG RPIPVRLEAL PQVESQVAAA
1060 1070 1080 1090 1100
RAWRERTGRT FLKKNSSHTL LQVLSPRTDI GVYGSGKNRR KKVKELIEKE
1110 1120 1130 1140 1150
KEKDLDLEPL SDLEEGLEET RDTAMVVAVF KEREQKEIEA MHSLRAANLA
1160 1170 1180 1190 1200
KMTMVDRIEE VKFCICRKTA SGFMLQCELC KDWFHNSCVP LPKSSSQKKG
1210 1220 1230 1240 1250
SSWQAKEVKF LCPLCMRSRR PRLETILSLL VSLQKLPVRL PEGEALQCLT
1260 1270 1280 1290 1300
ERAMSWQDRA RQALATDELS SALAKLSVLS QRMVEQAARE KTEKIISAEL
1310 1320 1330 1340 1350
QKAAANPDLQ GHLPSFQQSA FNRVVSSVSS SPRQTMDYDD EETDSDEDIR
1360 1370 1380 1390 1400
ETYGYDMKDT ASVKSSSSLE PNLFCDEEIP IKSEEVVTHM WTAPSFCAEH
1410 1420 1430 1440 1450
AYSSASKSCS QGSSTPRKQP RKSPLVPRSL EPPVLELSPG AKAQLEELMM
1460 1470 1480 1490 1500
VGDLLEVSLD ETQHIWRILQ ATHPPSEDRF LHIMEDDSME EKPLKVKGKD
1510 1520 1530 1540 1550
SSEKKRKRKL EKVEQLFGEG KQKSKELKKM DKPRKKKLKL GADKSKELNK
1560 1570 1580 1590 1600
LAKKLAKEEE RKKKKEKAAA AKVELVKEST EKKREKKVLD IPSKYDWSGA
1610 1620 1630 1640 1650
EESDDENAVC AAQNCQRPCK DKVDWVQCDG GCDEWFHQVC VGVSPEMAEN
1660 1670 1680 1690
EDYICINCAK KQGPVSPGPA PPPSFIMSYK LPMEDLKETS
Length:1,690
Mass (Da):192,095
Last modified:November 25, 2008 - 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:iFCF6DC22DEF001DF
GO
Isoform 2 (identifier: P29375-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1623-1690: VDWVQCDGGC...LPMEDLKETS → GVVFVTEEERDKKY

Show »
Length:1,636
Mass (Da):186,289
Checksum:iF308F907C2F899E0
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7EV89E7EV89_HUMAN
Lysine-specific demethylase 5A
KDM5A
715Annotation 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>
F5GZR8F5GZR8_HUMAN
Lysine-specific demethylase 5A
KDM5A
131Annotation 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>
F5GZ99F5GZ99_HUMAN
Lysine-specific demethylase 5A
KDM5A
126Annotation 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>
F5H322F5H322_HUMAN
Lysine-specific demethylase 5A
KDM5A
122Annotation 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 AAB28544 differs from that shown. Reason: Frameshift.Curated
The sequence BAE06081 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.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 conflicti1411Q → QVFFGK in AAB28544 (PubMed:8414517).Curated1
Sequence conflicti1547E → K in AAB28544 (PubMed:8414517).Curated1
Sequence conflicti1612 – 1614AQN → EPD in AAB28544 (PubMed:8414517).Curated3

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_032984865M → T. Corresponds to variant dbSNP:rs11062385Ensembl.1
Natural variantiVAR_0329851190P → A. Corresponds to variant dbSNP:rs2229353Ensembl.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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0357461623 – 1690VDWVQ…LKETS → GVVFVTEEERDKKY in isoform 2. 1 PublicationAdd BLAST68

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
S66431 mRNA Translation: AAB28544.1 Frameshift.
AB209999 mRNA Translation: BAE06081.1 Different initiation.
AC005844 Genomic DNA No translation available.
AC007406 Genomic DNA No translation available.
BC048307 mRNA Translation: AAH48307.1 Different termination.
BC053893 mRNA Translation: AAH53893.1 Different termination.
BC110916 mRNA Translation: AAI10917.1 Different termination.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS41736.1 [P29375-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
I78879

NCBI Reference Sequences

More...
RefSeqi
NP_001036068.1, NM_001042603.2 [P29375-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000399788; ENSP00000382688; ENSG00000073614 [P29375-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5927

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5927

UCSC genome browser

More...
UCSCi
uc001qif.3, human [P29375-1]

Keywords - Coding sequence diversityi

Alternative splicing, 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
S66431 mRNA Translation: AAB28544.1 Frameshift.
AB209999 mRNA Translation: BAE06081.1 Different initiation.
AC005844 Genomic DNA No translation available.
AC007406 Genomic DNA No translation available.
BC048307 mRNA Translation: AAH48307.1 Different termination.
BC053893 mRNA Translation: AAH53893.1 Different termination.
BC110916 mRNA Translation: AAI10917.1 Different termination.
CCDSiCCDS41736.1 [P29375-1]
PIRiI78879
RefSeqiNP_001036068.1, NM_001042603.2 [P29375-1]

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
2JXJNMR-A85-175[»]
2KGGNMR-A1609-1659[»]
2KGINMR-A1609-1659[»]
3GL6X-ray1.90A1609-1659[»]
5C11X-ray2.80A1609-1659[»]
5CEHX-ray3.14A12-797[»]
5E6HX-ray2.24A1-87[»]
A348-588[»]
5ISLX-ray1.69A1-87[»]
A348-588[»]
5IVBX-ray1.39A1-87[»]
A348-588[»]
5IVCX-ray1.57A1-87[»]
A348-588[»]
5IVEX-ray1.78A1-87[»]
A348-588[»]
5IVFX-ray1.68A1-87[»]
A348-588[»]
5IVJX-ray1.57A1-87[»]
A348-588[»]
5IVVX-ray1.85A1-87[»]
A348-588[»]
5IVYX-ray1.45A1-87[»]
A348-588[»]
5IW0X-ray1.63A1-87[»]
A348-588[»]
5IWFX-ray2.29A1-87[»]
A348-588[»]
5K4LX-ray3.18A/B12-797[»]
5V9PX-ray3.00A12-797[»]
5V9TX-ray3.05A/B12-797[»]
6BGUX-ray1.68A1-588[»]
6BGVX-ray1.59A1-588[»]
6BGWX-ray1.64A1-588[»]
6BGXX-ray1.88A1-588[»]
6BGYX-ray1.22A1-588[»]
6BGZX-ray1.69A1-588[»]
6BH0X-ray1.99A1-588[»]
6BH1X-ray1.93A1-588[»]
6BH2X-ray1.45A1-588[»]
6BH3X-ray1.70A1-588[»]
6BH4X-ray2.05A1-588[»]
6BH5X-ray1.65A1-588[»]
6DQ4X-ray1.39A1-588[»]
6DQ5X-ray1.89A1-588[»]
6DQ6X-ray1.59A1-588[»]
6DQ7X-ray1.85A1-588[»]
6DQ8X-ray1.46A1-588[»]
6DQ9X-ray1.75A1-588[»]
6DQAX-ray1.89A1-588[»]
6DQBX-ray1.79A1-588[»]
6DQCX-ray1.75A1-588[»]
6DQDX-ray1.99A1-588[»]
6DQEX-ray1.69A1-588[»]
6DQFX-ray1.69A1-588[»]
7KLONMR-A287-344[»]
7KLRNMR-A287-344[»]
BMRBiP29375
SMRiP29375
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111862, 50 interactors
DIPiDIP-472N
IntActiP29375, 23 interactors
MINTiP29375
STRINGi9606.ENSP00000382688

Chemistry databases

BindingDBiP29375
ChEMBLiCHEMBL2424504
GuidetoPHARMACOLOGYi2680

PTM databases

iPTMnetiP29375
PhosphoSitePlusiP29375
SwissPalmiP29375

Genetic variation databases

BioMutaiKDM5A
DMDMi215274124

Proteomic databases

EPDiP29375
jPOSTiP29375
MassIVEiP29375
MaxQBiP29375
PaxDbiP29375
PeptideAtlasiP29375
PRIDEiP29375
ProteomicsDBi54559 [P29375-1]
54560 [P29375-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
1751, 224 antibodies

The DNASU plasmid repository

More...
DNASUi
5927

Genome annotation databases

EnsembliENST00000399788; ENSP00000382688; ENSG00000073614 [P29375-1]
GeneIDi5927
KEGGihsa:5927
UCSCiuc001qif.3, human [P29375-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5927
DisGeNETi5927

GeneCards: human genes, protein and diseases

More...
GeneCardsi
KDM5A
HGNCiHGNC:9886, KDM5A
HPAiENSG00000073614, Low tissue specificity
MIMi180202, gene
neXtProtiNX_P29375
OpenTargetsiENSG00000073614
PharmGKBiPA34250
VEuPathDBiHostDB:ENSG00000073614

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1246, Eukaryota
GeneTreeiENSGT00940000157170
HOGENOMiCLU_000991_2_0_1
InParanoidiP29375
OMAiKWAPVAP
OrthoDBi664180at2759
PhylomeDBiP29375
TreeFamiTF106476

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000073614-MONOMER
BRENDAi1.14.11.67, 2681
PathwayCommonsiP29375
ReactomeiR-HSA-3214842, HDMs demethylate histones
SIGNORiP29375

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
5927, 13 hits in 1047 CRISPR screens

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

More...
ChiTaRSi
KDM5A, human
EvolutionaryTraceiP29375

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
JARID1A

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

More...
GenomeRNAii
5927
PharosiP29375, Tchem

Protein Ontology

More...
PROi
PR:P29375
RNActiP29375, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000073614, Expressed in peritoneum and 254 other tissues
ExpressionAtlasiP29375, baseline and differential
GenevisibleiP29375, HS

Family and domain databases

DisProtiDP02224
Gene3Di1.10.150.60, 1 hit
3.30.40.10, 3 hits
InterProiView protein in InterPro
IPR001606, ARID_dom
IPR036431, ARID_dom_sf
IPR003347, JmjC_dom
IPR003349, JmjN
IPR013637, Lys_sp_deMease-like_dom
IPR019786, Zinc_finger_PHD-type_CS
IPR004198, Znf_C5HC2
IPR011011, Znf_FYVE_PHD
IPR001965, Znf_PHD
IPR019787, Znf_PHD-finger
IPR013083, Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF01388, ARID, 1 hit
PF02373, JmjC, 1 hit
PF02375, JmjN, 1 hit
PF00628, PHD, 2 hits
PF08429, PLU-1, 1 hit
PF02928, zf-C5HC2, 1 hit
SMARTiView protein in SMART
SM00501, BRIGHT, 1 hit
SM00558, JmjC, 1 hit
SM00545, JmjN, 1 hit
SM00249, PHD, 3 hits
SUPFAMiSSF46774, SSF46774, 1 hit
SSF57903, SSF57903, 3 hits
PROSITEiView protein in PROSITE
PS51011, ARID, 1 hit
PS51184, JMJC, 1 hit
PS51183, JMJN, 1 hit
PS01359, ZF_PHD_1, 2 hits
PS50016, ZF_PHD_2, 3 hits

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKDM5A_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: P29375
Secondary accession number(s): A8MV76, Q4LE72, Q86XZ1
<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, 1992
Last sequence update: November 25, 2008
Last modified: September 29, 2021
This is version 206 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, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
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