Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 198 (13 Feb 2019)
Sequence version 2 (25 Nov 2008)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Histone acetyltransferase KAT6A

Gene

KAT6A

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 acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2. Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML.6 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 is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei680Proton donor/acceptorBy similarity1
<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 sitei684Acetyl-CoA1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 fingeri206 – 265PHD-type 1PROSITE-ProRule annotationAdd BLAST60
Zinc fingeri259 – 313PHD-type 2PROSITE-ProRule annotationAdd BLAST55
Zinc fingeri537 – 562C2HC MYST-typePROSITE-ProRule annotationAdd BLAST26

<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

  • acetyltransferase activity Source: UniProtKB
  • DNA binding Source: UniProtKB
  • H4 histone acetyltransferase activity Source: GO_Central
  • histone acetyltransferase activity Source: UniProtKB
  • histone binding Source: GO_Central
  • transcription coactivator activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

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, Acyltransferase, Chromatin regulator, Repressor, Transferase
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-3214847 HATs acetylate histones
R-HSA-6804758 Regulation of TP53 Activity through Acetylation

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q92794

<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:
Histone acetyltransferase KAT6A (EC:2.3.1.482 Publications)
Alternative name(s):
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3
Short name:
MYST-3
Monocytic leukemia zinc finger protein
Runt-related transcription factor-binding protein 2
Zinc finger protein 220
<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:KAT6A
Synonyms:MOZ, MYST3, RUNXBP2, ZNF220
<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 8

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000083168.9

Human Gene Nomenclature Database

More...
HGNCi
HGNC:13013 KAT6A

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
601408 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q92794

<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

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

Chromosomal aberrations involving KAT6A may be a cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13) with CREBBP (PubMed:8782817). Translocation t(8;22)(p11;q13) with EP300 (PubMed:10824998). KAT6A-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription (PubMed:11742995). Inversion inv(8)(p11;q13) generates the KAT6A-NCOA2 oncogene, which consists of the N-terminal part of KAT6A and the C-terminal part of NCOA2/TIF2. KAT6A-NCOA2 binds to CREBBP and disrupts its function in transcription activation (PubMed:12676584).4 Publications
A chromosomal aberration involving KAT6A is a cause of therapy-related myelodysplastic syndrome. Translocation t(2;8)(p23;p11.2) with ASXL2 generates a KAT6A-ASXL2 fusion protein.1 Publication
Mental retardation, autosomal dominant 32 (MRD32)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD32 patients manifest intellectual disability, dysmorphic facial features, delayed psychomotor development, and lack of speech.
See also OMIM:616268

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>Mutagenesisi543C → G: Abrogates HAT activity. 1 Publication1
Mutagenesisi545K → A: Reduced affinity for DNA. 1 Publication1
Mutagenesisi657G → E: Abrogates HAT activity. 1 Publication1
Mutagenesisi727I → E: Slightly reduced affinity for DNA. 1 Publication1
Mutagenesisi732H → D: Reduced affinity for DNA. 1 Publication1

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>Sitei813 – 814Breakpoint for translocation to form KAT6A-ASXL22
Sitei1117 – 1118Breakpoint for translocation to form KAT6A-EP300 and KAT6A-NCOA22
Sitei1546 – 1547Breakpoint for translocation to form KAT6A-CREBBP2

Keywords - Diseasei

Mental retardation, Proto-oncogene

Organism-specific databases

DisGeNET

More...
DisGeNETi
7994

MalaCards human disease database

More...
MalaCardsi
KAT6A
MIMi616268 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000083168

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

More...
Orphaneti
370026 Acute myeloid leukemia with t(8;16)(p11;p13) translocation
457193 Autosomal dominant intellectual disability-craniofacial anomalies-cardiac defects syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA37592

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3774298

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
KAT6A

Domain mapping of disease mutations (DMDM)

More...
DMDMi
215274095

<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_00000515721 – 2004Histone acetyltransferase KAT6AAdd BLAST2004

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 residuei172N6-acetyllysineBy similarity1
Modified residuei350N6-acetyllysineCombined sources1
Modified residuei355N6-acetyllysineCombined sources1
Modified residuei369Phosphothreonine; by PKB/AKT11 Publication1
Modified residuei420PhosphoserineCombined sources1
Modified residuei473PhosphoserineCombined sources1
Modified residuei604N6-acetyllysine; by autocatalysis1 Publication1
Modified residuei787PhosphoserineBy similarity1
Modified residuei812PhosphoserineCombined sources1
Modified residuei815N6-acetyllysineBy similarity1
<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-linki834Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei899PhosphotyrosineBy similarity1
Modified residuei941PhosphoserineCombined sources1
Modified residuei954PhosphoserineCombined sources1
Modified residuei974PhosphoserineCombined sources1
Modified residuei1007N6-acetyllysineCombined sources1
Modified residuei1089PhosphoserineCombined sources1
Modified residuei1090PhosphoserineCombined sources1
Modified residuei1113PhosphoserineCombined sources1
Cross-linki1342Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

<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

Autoacetylation at Lys-604 is required for proper function (By similarity). Autoacetylated.By similarity1 Publication
Phosphorylation at Thr-369 by PKB/AKT1 inhibits its interaction with PML and negatively regulates its acetylation activity towards p53/TP53.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q92794

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q92794

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q92794

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

More...
PaxDbi
Q92794

PeptideAtlas

More...
PeptideAtlasi
Q92794

PRoteomics IDEntifications database

More...
PRIDEi
Q92794

ProteomicsDB human proteome resource

More...
ProteomicsDBi
75473

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q92794

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

More...
PhosphoSitePlusi
Q92794

<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
ENSG00000083168 Expressed in 244 organ(s), highest expression level in cerebral cortex

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q92794 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q92794 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB017023
HPA063266
HPA065052

<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

Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. Interacts with RUNX1; phosphorylation of RUNX1 enhances the interaction. Interacts with RUNX2. Interacts with p53/TP53. Interacts with PML (isoform PML-4) and this interaction positively regulates its acetylation activity towards p53/TP53.6 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
113703, 44 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-727 MOZ1 histone acetyltransferase complex
CPX-733 MOZ2 histone acetyltransferase complex
CPX-736 MOZ3 histone acetyltransferase complex

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q92794

Protein interaction database and analysis system

More...
IntActi
Q92794, 22 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000265713

<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

12004
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1M36NMR-A533-563[»]
2LN0NMR-A204-313[»]
2OZUX-ray2.30A497-780[»]
2RC4X-ray3.00A501-784[»]
3V43X-ray1.47A204-313[»]
4LJNX-ray3.00A194-323[»]
4LK9X-ray1.60A194-323[»]
4LKAX-ray1.61A194-323[»]
4LLBX-ray2.50A/B194-323[»]
5B75X-ray1.70A194-323[»]
5B76X-ray1.65A194-323[»]
5B77X-ray1.55A194-323[»]
5B78X-ray1.40A194-323[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q92794

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

More...
SMRi
Q92794

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
Q92794

<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>Domaini95 – 171H15PROSITE-ProRule annotationAdd BLAST77
Domaini504 – 778MYST-type HATPROSITE-ProRule annotationAdd BLAST275

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 144Required for activation of RUNX1-1Add BLAST144
Regioni52 – 166Required for nuclear localizationAdd BLAST115
Regioni144 – 664Interaction with PML1 PublicationAdd BLAST521
Regioni312 – 664Interaction with RUNX1-1Add BLAST353
Regioni488 – 778CatalyticAdd BLAST291
Regioni507 – 810Mediates interaction with BRPF1, required for histone H3 acetyltransferase activity1 PublicationAdd BLAST304
Regioni645 – 649Acetyl-CoA binding1 Publication5
Regioni654 – 660Acetyl-CoA binding1 Publication7
Regioni1517 – 1741Interaction with PML1 PublicationAdd BLAST225
Regioni1517 – 1642Interaction with RUNX1-2Add BLAST126
Regioni1913 – 1948Required for activation of RUNX1-2Add BLAST36

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi371 – 379Poly-Ser9
Compositional biasi788 – 801Poly-GluAdd BLAST14
Compositional biasi989 – 995Poly-Glu7
Compositional biasi1019 – 1026Poly-Arg8
Compositional biasi1069 – 1078Poly-Glu10
Compositional biasi1147 – 1150Poly-Lys4
Compositional biasi1221 – 1242Glu-richAdd BLAST22
Compositional biasi1267 – 1302Glu-richAdd BLAST36
Compositional biasi1411 – 1414Poly-Glu4
Compositional biasi1593 – 1597Poly-Ser5
Compositional biasi1643 – 1704Gln/Pro-richAdd BLAST62
Compositional biasi1897 – 1977Met-richAdd BLAST81

<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 N-terminus is involved in transcriptional activation while the C-terminus is involved in transcriptional repression.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri206 – 265PHD-type 1PROSITE-ProRule annotationAdd BLAST60
Zinc fingeri259 – 313PHD-type 2PROSITE-ProRule annotationAdd BLAST55
Zinc fingeri537 – 562C2HC MYST-typePROSITE-ProRule annotationAdd BLAST26

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2747 Eukaryota
COG5027 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156962

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000234365

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG052563

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q92794

KEGG Orthology (KO)

More...
KOi
K11305

Identification of Orthologs from Complete Genome Data

More...
OMAi
ICQICRP

Database of Orthologous Groups

More...
OrthoDBi
629545at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q92794

TreeFam database of animal gene trees

More...
TreeFami
TF106483

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.10, 1 hit
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016181 Acyl_CoA_acyltransferase
IPR002717 HAT_MYST-type
IPR005818 Histone_H1/H5_H15
IPR031280 KAT6A
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
IPR040706 Zf-MYST
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR013083 Znf_RING/FYVE/PHD

The PANTHER Classification System

More...
PANTHERi
PTHR10615:SF26 PTHR10615:SF26, 2 hits

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01853 MOZ_SAS, 1 hit
PF00628 PHD, 1 hit
PF17772 zf-MYST, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00526 H15, 1 hit
SM00249 PHD, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46785 SSF46785, 1 hit
SSF55729 SSF55729, 1 hit
SSF57903 SSF57903, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51504 H15, 1 hit
PS51726 MYST_HAT, 1 hit
PS01359 ZF_PHD_1, 1 hit
PS50016 ZF_PHD_2, 2 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>.<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 7 potential isoforms that are computationally mapped.Show allAlign All

Q92794-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVKLANPLYT EWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRKTVLEQ
60 70 80 90 100
LELSVKDGTI LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDNKQNVDWN
110 120 130 140 150
KLIKRAVEGL AESGGSTLKS IERFLKGQKD VSALFGGSAA SGFHQQLRLA
160 170 180 190 200
IKRAIGHGRL LKDGPLYRLN TKATNVDGKE SCESLSCLPP VSLLPHEKDK
210 220 230 240 250
PVAEPIPICS FCLGTKEQNR EKKPEELISC ADCGNSGHPS CLKFSPELTV
260 270 280 290 300
RVKALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM
310 320 330 340 350
PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YTNPIGRPKN RLKKQNTVSK
360 370 380 390 400
GPFSKVRTGP GRGRKRKITL SSQSASSSSE EGYLERIDGL DFCRDSNVSL
410 420 430 440 450
KFNKKTKGLI DGLTKFFTPS PDGRKARGEV VDYSEQYRIR KRGNRKSSTS
460 470 480 490 500
DWPTDNQDGW DGKQENEERL FGSQEIMTEK DMELFRDIQE QALQKVGVTG
510 520 530 540 550
PPDPQVRCPS VIEFGKYEIH TWYSSPYPQE YSRLPKLYLC EFCLKYMKSR
560 570 580 590 600
TILQQHMKKC GWFHPPANEI YRKNNISVFE VDGNVSTIYC QNLCLLAKLF
610 620 630 640 650
LDHKTLYYDV EPFLFYVLTQ NDVKGCHLVG YFSKEKHCQQ KYNVSCIMIL
660 670 680 690 700
PQYQRKGYGR FLIDFSYLLS KREGQAGSPE KPLSDLGRLS YMAYWKSVIL
710 720 730 740 750
ECLYHQNDKQ ISIKKLSKLT GICPQDITST LHHLRMLDFR SDQFVIIRRE
760 770 780 790 800
KLIQDHMAKL QLNLRPVDVD PECLRWTPVI VSNSVVSEEE EEEAEEGENE
810 820 830 840 850
EPQCQERELE ISVGKSVSHE NKEQDSYSVE SEKKPEVMAP VSSTRLSKQV
860 870 880 890 900
LPHDSLPANS QPSRRGRWGR KNRKTQERFG DKDSKLLLEE TSSAPQEQYG
910 920 930 940 950
ECGEKSEATQ EQYTESEEQL VASEEQPSQD GKPDLPKRRL SEGVEPWRGQ
960 970 980 990 1000
LKKSPEALKC RLTEGSERLP RRYSEGDRAV LRGFSESSEE EEEPESPRSS
1010 1020 1030 1040 1050
SPPILTKPTL KRKKPFLHRR RRVRKRKHHN SSVVTETISE TTEVLDEPFE
1060 1070 1080 1090 1100
DSDSERPMPR LEPTFEIDEE EEEEDENELF PREYFRRLSS QDVLRCQSSS
1110 1120 1130 1140 1150
KRKSKDEEED EESDDADDTP ILKPVSLLRK RDVKNSPLEP DTSTPLKKKK
1160 1170 1180 1190 1200
GWPKGKSRKP IHWKKRPGRK PGFKLSREIM PVSTQACVIE PIVSIPKAGR
1210 1220 1230 1240 1250
KPKIQESEET VEPKEDMPLP EERKEEEEMQ AEAEEAEEGE EEDAASSEVP
1260 1270 1280 1290 1300
AASPADSSNS PETETKEPEV EEEEEKPRVS EEQRQSEEEQ QELEEPEPEE
1310 1320 1330 1340 1350
EEDAAAETAQ NDDHDADDED DGHLESTKKK ELEEQPTRED VKEEPGVQES
1360 1370 1380 1390 1400
FLDANMQKSR EKIKDKEETE LDSEEEQPSH DTSVVSEQMA GSEDDHEEDS
1410 1420 1430 1440 1450
HTKEELIELK EEEEIPHSEL DLETVQAVQS LTQEESSEHE GAYQDCEETL
1460 1470 1480 1490 1500
AACQTLQSYT QADEDPQMSM VEDCHASEHN SPISSVQSHP SQSVRSVSSP
1510 1520 1530 1540 1550
NVPALESGYT QISPEQGSLS APSMQNMETS PMMDVPSVSD HSQQVVDSGF
1560 1570 1580 1590 1600
SDLGSIESTT ENYENPSSYD STMGGSICGN SSSQSSCSYG GLSSSSSLTQ
1610 1620 1630 1640 1650
SSCVVTQQMA SMGSSCSMMQ QSSVQPAANC SIKSPQSCVV ERPPSNQQQQ
1660 1670 1680 1690 1700
PPPPPPQQPQ PPPPQPQPAP QPPPPQQQPQ QQPQPQPQQP PPPPPPQQQP
1710 1720 1730 1740 1750
PLSQCSMNNS FTPAPMIMEI PESGSTGNIS IYERIPGDFG AGSYSQPSAT
1760 1770 1780 1790 1800
FSLAKLQQLT NTIMDPHAMP YSHSPAVTSY ATSVSLSNTG LAQLAPSHPL
1810 1820 1830 1840 1850
AGTPQAQATM TPPPNLASTT MNLTSPLLQC NMSATNIGIP HTQRLQGQMP
1860 1870 1880 1890 1900
VKGHISIRSK SAPLPSAAAH QQQLYGRSPS AVAMQAGPRA LAVQRGMNMG
1910 1920 1930 1940 1950
VNLMPTPAYN VNSMNMNTLN AMNSYRMTQP MMNSSYHSNP AYMNQTAQYP
1960 1970 1980 1990 2000
MQMQMGMMGS QAYTQQPMQP NPHGNMMYTG PSHHSYMNAA GVPKQSLNGP

YMRR
Length:2,004
Mass (Da):225,028
Last modified:November 25, 2008 - 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:i78357EFAC4698A5F
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 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A5PLL3A5PLL3_HUMAN
Histone acetyltransferase
KAT6A MYST3
815Annotation score:

Annotation score:3 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>
A0A3B3IS53A0A3B3IS53_HUMAN
Histone acetyltransferase
KAT6A
1,677Annotation score:

Annotation score:3 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>
A0A3B3ITI3A0A3B3ITI3_HUMAN
Histone acetyltransferase
KAT6A
1,565Annotation score:

Annotation score:2 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>
A0A3B3ISU5A0A3B3ISU5_HUMAN
Histone acetyltransferase KAT6A
KAT6A
348Annotation score:

Annotation score:2 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>
A0A3F2YNX6A0A3F2YNX6_HUMAN
Histone acetyltransferase
KAT6A
2,006Annotation score:

Annotation score:2 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>
C9JJY6C9JJY6_HUMAN
Histone acetyltransferase KAT6A
KAT6A
214Annotation score:

Annotation score:2 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>
A0A3B3ISZ3A0A3B3ISZ3_HUMAN
Histone acetyltransferase KAT6A
KAT6A
97Annotation 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 conflicti401K → R in AAC50662 (PubMed:8782817).Curated1
Sequence conflicti401K → R in BAD00088 (Ref. 3) 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_047548134L → S. Corresponds to variant dbSNP:rs3824276Ensembl.1

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
U47742 mRNA Translation: AAC50662.1
AC090571 Genomic DNA No translation available.
AB084281 mRNA Translation: BAD00088.1 Different termination.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS6124.1

NCBI Reference Sequences

More...
RefSeqi
NP_006757.2, NM_006766.4
XP_016869352.1, XM_017013863.1
XP_016869353.1, XM_017013864.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.491577

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000265713; ENSP00000265713; ENSG00000083168
ENST00000396930; ENSP00000380136; ENSG00000083168

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7994

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:7994

UCSC genome browser

More...
UCSCi
uc003xon.4 human

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

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

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47742 mRNA Translation: AAC50662.1
AC090571 Genomic DNA No translation available.
AB084281 mRNA Translation: BAD00088.1 Different termination.
CCDSiCCDS6124.1
RefSeqiNP_006757.2, NM_006766.4
XP_016869352.1, XM_017013863.1
XP_016869353.1, XM_017013864.1
UniGeneiHs.491577

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M36NMR-A533-563[»]
2LN0NMR-A204-313[»]
2OZUX-ray2.30A497-780[»]
2RC4X-ray3.00A501-784[»]
3V43X-ray1.47A204-313[»]
4LJNX-ray3.00A194-323[»]
4LK9X-ray1.60A194-323[»]
4LKAX-ray1.61A194-323[»]
4LLBX-ray2.50A/B194-323[»]
5B75X-ray1.70A194-323[»]
5B76X-ray1.65A194-323[»]
5B77X-ray1.55A194-323[»]
5B78X-ray1.40A194-323[»]
ProteinModelPortaliQ92794
SMRiQ92794
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113703, 44 interactors
ComplexPortaliCPX-727 MOZ1 histone acetyltransferase complex
CPX-733 MOZ2 histone acetyltransferase complex
CPX-736 MOZ3 histone acetyltransferase complex
CORUMiQ92794
IntActiQ92794, 22 interactors
STRINGi9606.ENSP00000265713

Chemistry databases

ChEMBLiCHEMBL3774298

PTM databases

iPTMnetiQ92794
PhosphoSitePlusiQ92794

Polymorphism and mutation databases

BioMutaiKAT6A
DMDMi215274095

Proteomic databases

EPDiQ92794
jPOSTiQ92794
MaxQBiQ92794
PaxDbiQ92794
PeptideAtlasiQ92794
PRIDEiQ92794
ProteomicsDBi75473

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
7994
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265713; ENSP00000265713; ENSG00000083168
ENST00000396930; ENSP00000380136; ENSG00000083168
GeneIDi7994
KEGGihsa:7994
UCSCiuc003xon.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7994
DisGeNETi7994
EuPathDBiHostDB:ENSG00000083168.9

GeneCards: human genes, protein and diseases

More...
GeneCardsi
KAT6A
HGNCiHGNC:13013 KAT6A
HPAiCAB017023
HPA063266
HPA065052
MalaCardsiKAT6A
MIMi601408 gene
616268 phenotype
neXtProtiNX_Q92794
OpenTargetsiENSG00000083168
Orphaneti370026 Acute myeloid leukemia with t(8;16)(p11;p13) translocation
457193 Autosomal dominant intellectual disability-craniofacial anomalies-cardiac defects syndrome
PharmGKBiPA37592

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2747 Eukaryota
COG5027 LUCA
GeneTreeiENSGT00940000156962
HOGENOMiHOG000234365
HOVERGENiHBG052563
InParanoidiQ92794
KOiK11305
OMAiICQICRP
OrthoDBi629545at2759
PhylomeDBiQ92794
TreeFamiTF106483

Enzyme and pathway databases

ReactomeiR-HSA-3214847 HATs acetylate histones
R-HSA-6804758 Regulation of TP53 Activity through Acetylation
SIGNORiQ92794

Miscellaneous databases

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

More...
ChiTaRSi
KAT6A human
EvolutionaryTraceiQ92794

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
MYST3

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

More...
GenomeRNAii
7994

Protein Ontology

More...
PROi
PR:Q92794

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000083168 Expressed in 244 organ(s), highest expression level in cerebral cortex
ExpressionAtlasiQ92794 baseline and differential
GenevisibleiQ92794 HS

Family and domain databases

Gene3Di1.10.10.10, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR016181 Acyl_CoA_acyltransferase
IPR002717 HAT_MYST-type
IPR005818 Histone_H1/H5_H15
IPR031280 KAT6A
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
IPR040706 Zf-MYST
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR013083 Znf_RING/FYVE/PHD
PANTHERiPTHR10615:SF26 PTHR10615:SF26, 2 hits
PfamiView protein in Pfam
PF01853 MOZ_SAS, 1 hit
PF00628 PHD, 1 hit
PF17772 zf-MYST, 1 hit
SMARTiView protein in SMART
SM00526 H15, 1 hit
SM00249 PHD, 2 hits
SUPFAMiSSF46785 SSF46785, 1 hit
SSF55729 SSF55729, 1 hit
SSF57903 SSF57903, 2 hits
PROSITEiView protein in PROSITE
PS51504 H15, 1 hit
PS51726 MYST_HAT, 1 hit
PS01359 ZF_PHD_1, 1 hit
PS50016 ZF_PHD_2, 2 hits

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 nameiKAT6A_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: Q92794
Secondary accession number(s): Q76L81
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 25, 2008
Last modified: February 13, 2019
This is version 198 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. 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