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UniProtKB - O95251 (KAT7_HUMAN)

Entry version 185 (02 Dec 2020)
Sequence version 1 (01 May 1999)
Previous versions | rss
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Protein

Histone acetyltransferase KAT7

Gene

KAT7

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

Catalytic subunit of histone acetyltransferase HBO1 complexes, which specifically mediate acetylation of histone H3 at 'Lys-14' (H3K14ac), thereby regulating various processes, such as gene transcription, protein ubiquitination, immune regulation, stem cell pluripotent and self-renewal maintenance and embryonic development (PubMed:16387653, PubMed:21753189, PubMed:24065767, PubMed:26620551, PubMed:31767635, PubMed:31827282). Some complexes also catalyze acetylation of histone H4 at 'Lys-5', 'Lys-8' and 'Lys-12' (H4K5ac, H4K8ac and H4K12ac, respectively), regulating DNA replication initiation, regulating DNA replication initiation (PubMed:10438470, PubMed:19187766, PubMed:20129055, PubMed:24065767). Specificity of the HBO1 complexes is determined by the scaffold subunit: complexes containing BRPF scaffold (BRPF1, BRD1/BRPF2 or BRPF3) direct KAT7/HBO1 specificity towards H3K14ac, while complexes containing JADE (JADE1, JADE2 and JADE3) scaffold direct KAT7/HBO1 specificity towards histone H4 (PubMed:19187766, PubMed:20129055, PubMed:24065767, PubMed:26620551). H3K14ac promotes transcriptional elongation by facilitating the processivity of RNA polymerase II (PubMed:31827282). Acts as a key regulator of hematopoiesis by forming a complex with BRD1/BRPF2, directing KAT7/HBO1 specificity towards H3K14ac and promoting erythroid differentiation (PubMed:21753189). H3K14ac is also required for T-cell development (By similarity). KAT7/HBO1-mediated acetylation facilitates two consecutive steps, licensing and activation, in DNA replication initiation: H3K14ac facilitates the activation of replication origins, and histone H4 acetylation (H4K5ac, H4K8ac and H4K12ac) facilitates chromatin loading of MCM complexes, promoting DNA replication licensing (PubMed:10438470, PubMed:11278932, PubMed:18832067, PubMed:19187766, PubMed:20129055, PubMed:21856198, PubMed:24065767, PubMed:26620551). Acts as a positive regulator of centromeric CENPA assembly: recruited to centromeres and mediates histone acetylation, thereby preventing centromere inactivation mediated by SUV39H1, possibly by increasing histone turnover/exchange (PubMed:27270040). Involved in nucleotide excision repair: phosphorylation by ATR in response to ultraviolet irradiation promotes its localization to DNA damage sites, where it mediates histone acetylation to facilitate recruitment of XPC at the damaged DNA sites (PubMed:28719581). Acts as an inhibitor of NF-kappa-B independently of its histone acetyltransferase activity (PubMed:16997280).By similarity15 Publications
Plays a central role in the maintenance of leukemia stem cells in acute myeloid leukemia (AML) (PubMed:31827282). Acts by mediating acetylation of histone H3 at 'Lys-14' (H3K14ac), thereby facilitating the processivity of RNA polymerase II to maintain the high expression of key genes, such as HOXA9 and HOXA10 that help to sustain the functional properties of leukemia stem cells (PubMed:31827282).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">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

Histone acetyltransferase activity is inhibited by GMNN in the context of a complex with CDT1, inhibiting histone H4 acetylation and DNA replication licensing (PubMed:20129055). Selectively inhibited by WM-3835 (N'-(4-fluoro-5-methyl-[1,1'-biphenyl]-3-carbonyl)-3- hydroxybenzenesulfonohydrazide) inhibitor (PubMed:31827282).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi368ZincCombined sources2 Publications1
Metal bindingi371ZincCombined sources2 Publications1
Metal bindingi384ZincCombined sources2 Publications1
Metal bindingi388ZincCombined sources2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei508Proton donor/acceptor1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei512acetyl-CoACombined sources2 Publications1
Binding sitei518WM-3835 inhibitorCombined sources1 Publication1
Binding sitei521acetyl-CoACombined sources2 Publications1
Binding sitei525WM-3835 inhibitorCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 fingeri176 – 219CCHHC-typePROSITE-ProRule annotationAdd BLAST44
Zinc fingeri365 – 390C2HC 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

Molecular functionAcyltransferase, Chromatin regulator, Transferase
Biological processDNA damage, DNA repair, DNA replication, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		O95251

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-3214847, HATs acetylate histones

SIGNOR Signaling Network Open Resource

More...SIGNORi		O95251

<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%5Fand%5Ftaxonomy%5Fsection">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 KAT7Curated (EC:2.3.1.485 Publications)
Alternative name(s):
Histone acetyltransferase binding to ORC12 Publications
Lysine acetyltransferase 71 Publication
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 21 Publication
Short name:
MYST-21 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:KAT71 PublicationImported
Synonyms:HBO12 Publications, HBOa1 Publication, MYST21 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 17

Organism-specific databases

Eukaryotic Pathogen and Host Database Resources

More...EuPathDBi		HostDB:ENSG00000136504.11

Human Gene Nomenclature Database

More...HGNCi		HGNC:17016, KAT7

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		609880, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_O95251

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Nucleus

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi50 – 53SQSS → AQSA: Impaired phosphorylation by ATR, leading to decreased ubiquitination and increased stability in response to DNA damage. 1 Publication4
Mutagenesisi57S → A: Leads to cell cycle arrest in the G1/S phase. 1 Publication1
Mutagenesisi338K → R: Decreases ubiquitination. 1 Publication1
Mutagenesisi371C → A: No interaction with MCM2 and ORC1. 1 Publication1
Mutagenesisi485G → A: Abolishes histone acetyltransferase activity. 2 Publications1
Mutagenesisi508E → A: Abolished histone acetyltransferase activity. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		11143

Open Targets

More...OpenTargetsi		ENSG00000136504

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA134886407

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		O95251, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3774299

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		KAT7

<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_00000515691 – 611Histone acetyltransferase KAT7Add BLAST611

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 residuei10PhosphoserineCombined sources1
Modified residuei50Phosphoserine; by ATRCombined sources2 Publications1
Modified residuei53Phosphoserine; by ATR2 Publications1
Modified residuei57Phosphoserine; by PLK1Combined sources1 Publication1
Modified residuei64PhosphoserineCombined sources1
Modified residuei85Phosphothreonine; by CDK1Combined sources1 Publication1
Modified residuei88Phosphothreonine; by CDK1Combined sources1 Publication1
Modified residuei102PhosphoserineCombined sources1
Modified residuei104PhosphothreonineBy similarity1
Modified residuei111PhosphoserineCombined sources1
Modified residuei124PhosphoserineCombined sources1
Modified residuei128PhosphothreonineBy similarity1
Modified residuei158PhosphoserineCombined sources1
Modified residuei162PhosphoserineCombined sources1
Modified residuei164PhosphoserineCombined sources1
Modified residuei178PhosphoserineCombined sources1
Modified residuei199N6-acetyllysineCombined sources1
Modified residuei277N6-acetyllysineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki323Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki338Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei432N6-acetyllysine; by autocatalysisBy similarity1
Modified residuei506PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Phosphorylated at Ser-50 and Ser-53 by ATR in response to DNA damage, promoting its ubiquitination by the CRL4(DDB2) complex and subsequent degradation (PubMed:26572825). Phosphorylation at Ser-50 and Ser-53 by ATR in response to ultraviolet-induced DNA, promotes localization to DNA damage sites (PubMed:28719581). Phosphorylation at Ser-57 by PLK1 during mitosis seems important for prereplicative complex formation and DNA replication licensing, and requires prior phosphorylation at Thr-85 and Thr-88 by CDK1 (PubMed:18250300). Phosphorylated by MAP2K1, which accelerates its degradation (By similarity).By similarity3 Publications
Ubiquitinated at Lys-338, leading to proteasomal degradation (PubMed:23319590). Ubiquitinated by the CRL4(DDB2) complex following phosphorylation by ATR, leading to its subsequent degradation (PubMed:26572825).2 Publications
Autoacetylation at Lys-432 is required for proper function.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		O95251

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O95251

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		O95251

MaxQB - The MaxQuant DataBase

More...MaxQBi		O95251

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

More...PaxDbi		O95251

PeptideAtlas

More...PeptideAtlasi		O95251

PRoteomics IDEntifications database

More...PRIDEi		O95251

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		17693
33968
50746 [O95251-1]
50747 [O95251-2]
50748 [O95251-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O95251

MetOSite database of methionine sulfoxide sites

More...MetOSitei		O95251

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

More...PhosphoSitePlusi		O95251

SwissPalm database of S-palmitoylation events

More...SwissPalmi		O95251

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

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

Ubiquitously expressed, with highest levels in testis.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000136504, Expressed in testis and 234 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		O95251, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O95251, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000136504, 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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the HBO1 complex composed of KAT7/HBO1, MEAF6, ING4 or ING5, and one scaffold subunit: complexes containing BRPF scaffold (BRPF1, BRD1/BRPF2 or BRPF3) direct KAT7/HBO1 specificity towards H3K14ac, while complexes containing JADE scaffold (JADE1, JADE2 and JADE3) mediate acetylation of histone H4 (PubMed:16387653, PubMed:19187766, PubMed:20129055, PubMed:21753189, PubMed:24065767, PubMed:26620551, PubMed:29382722).

Interacts with MCM2 and ORC1 (PubMed:10438470, PubMed:11278932, PubMed:16387653).

Interacts with the androgen receptor (AR); in the presence of dihydrotestosterone (PubMed:10930412).

Interacts with CDT1 (PubMed:18832067).

Interacts with MAP2K1 and CUL1 (By similarity).

Interacts with p53/TP53; leading to inhibit histone acetyltransferase activity (PubMed:17954561).

Interacts with MIS18BP1 (PubMed:27270040).

By similarity13 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		116315, 87 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-718, HBO1-4.1 histone acetyltransferase complex
CPX-719, HBO1-4.2 histone acetyltransferase complex
CPX-720, HBO1-4.3 histone acetyltransferase complex
CPX-721, HBO1-5.1 histone acetyltransferase complex
CPX-722, HBO1-5.2 histone acetyltransferase complex
CPX-723, HBO1-5.3 histone acetyltransferase complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		O95251

Database of interacting proteins

More...DIPi		DIP-29697N

Protein interaction database and analysis system

More...IntActi		O95251, 62 interactors

Molecular INTeraction database

More...MINTi		O95251

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000259021

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		O95251, 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

1611
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		O95251

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">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>Domaini332 – 607MYST-type HATPROSITE-ProRule annotationAdd BLAST276

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>Regioni475 – 477acetyl-CoA bindingCombined sources2 Publications3
Regioni483 – 488acetyl-CoA bindingCombined sources2 Publications6
Regioni483 – 488WM-3835 inhibitor bindingCombined sources1 Publication6

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 biasi10 – 57Ser-richAdd BLAST48

<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 C2HC MYST-type zinc finger is required for interaction with MCM2 and ORC1.1 Publication
The N-terminus is involved in transcriptional repression, while the C-terminus mediates AR-interaction.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 fingeri176 – 219CCHHC-typePROSITE-ProRule annotationAdd BLAST44
Zinc fingeri365 – 390C2HC MYST-typePROSITE-ProRule annotationAdd BLAST26

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2747, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157744

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_011815_6_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O95251

Identification of Orthologs from Complete Genome Data

More...OMAi		XVRAQSR

Database of Orthologous Groups

More...OrthoDBi		629545at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O95251

TreeFam database of animal gene trees

More...TreeFami		TF317619

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.10.10, 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
IPR036388, WH-like_DNA-bd_sf
IPR040706, Zf-MYST
IPR002515, Znf_C2H2C
IPR036060, Znf_C2H2C_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01853, MOZ_SAS, 1 hit
PF01530, zf-C2HC, 1 hit
PF17772, zf-MYST, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF103637, SSF103637, 1 hit
SSF55729, SSF55729, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51726, MYST_HAT, 1 hit
PS51802, ZF_CCHHC, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">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 (5+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 5 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 5 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O95251-1) [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
MPRRKRNAGS SSDGTEDSDF STDLEHTDSS ESDGTSRRSA RVTRSSARLS 
        60         70         80         90        100
QSSQDSSPVR NLQSFGTEEP AYSTRRVTRS QQQPTPVTPK KYPLRQTRSS 
       110        120        130        140        150
GSETEQVVDF SDRETKNTAD HDESPPRTPT GNAPSSESDI DISSPNVSHD 
       160        170        180        190        200
ESIAKDMSLK DSGSDLSHRP KRRRFHESYN FNMKCPTPGC NSLGHLTGKH 
       210        220        230        240        250
ERHFSISGCP LYHNLSADEC KVRAQSRDKQ IEERMLSHRQ DDNNRHATRH 
       260        270        280        290        300
QAPTERQLRY KEKVAELRKK RNSGLSKEQK EKYMEHRQTY GNTREPLLEN 
       310        320        330        340        350
LTSEYDLDLF RRAQARASED LEKLRLQGQI TEGSNMIKTI AFGRYELDTW 
       360        370        380        390        400
YHSPYPEEYA RLGRLYMCEF CLKYMKSQTI LRRHMAKCVW KHPPGDEIYR 
       410        420        430        440        450
KGSISVFEVD GKKNKIYCQN LCLLAKLFLD HKTLYYDVEP FLFYVMTEAD 
       460        470        480        490        500
NTGCHLIGYF SKEKNSFLNY NVSCILTMPQ YMRQGYGKML IDFSYLLSKV 
       510        520        530        540        550
EEKVGSPERP LSDLGLISYR SYWKEVLLRY LHNFQGKEIS IKEISQETAV 
       560        570        580        590        600
NPVDIVSTLQ ALQMLKYWKG KHLVLKRQDL IDEWIAKEAK RSNSNKTMDP 
       610 
SCLKWTPPKG T
Length:611
Mass (Da):70,642
Last modified:May 1, 1999 - v1
<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:i8368E7C4F07D8D7C
GO
Isoform 2 (identifier: O95251-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     114-193: Missing.
     222-251: Missing.

Show »
Length:501
Mass (Da):58,136
Checksum:i005414956B922380
GO
Isoform 3 (identifier: O95251-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     55-113: Missing.
     114-193: Missing.
     222-251: Missing.

Show »
Length:442
Mass (Da):51,440
Checksum:iEF5AA3D8E63B35D0
GO
Isoform 4 (identifier: O95251-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     222-251: Missing.

Show »
Length:581
Mass (Da):66,947
Checksum:i30A3E4C3E47EFBED
GO
Isoform 5 (identifier: O95251-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     55-113: Missing.
     114-193: Missing.

Show »
Length:472
Mass (Da):55,135
Checksum:i906F630E44BAFD2B
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7EUP3E7EUP3_HUMAN
Histone acetyltransferase
KAT7
425Annotation 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>
D6RFZ5D6RFZ5_HUMAN
Histone acetyltransferase KAT7
KAT7
16Annotation 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>
A0A6Q8PHH2A0A6Q8PHH2_HUMAN
Histone acetyltransferase KAT7
KAT7
524Annotation 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 conflicti38 – 44Missing in BAG57945 (PubMed:14702039).Curated7
Sequence conflicti41R → Q in BAG57346 (PubMed:14702039).Curated1

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_04255255 – 113Missing in isoform 3 and isoform 5. 1 PublicationAdd BLAST59
Alternative sequenceiVSP_042553114 – 193Missing in isoform 2, isoform 3 and isoform 5. 1 PublicationAdd BLAST80
Alternative sequenceiVSP_042554222 – 251Missing in isoform 2, isoform 3 and isoform 4. 1 PublicationAdd BLAST30

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
AF074606 mRNA Translation: AAC99368.1
AF140360 mRNA Translation: AAD42348.1
AF217502 mRNA Translation: AAL56649.1
AK023890 mRNA Translation: BAG51236.1
AK293976 mRNA Translation: BAG57346.1
AK294014 mRNA Translation: BAG57375.1
AK294052 mRNA Translation: BAG57401.1
AK294836 mRNA Translation: BAG57945.1
AC015795 Genomic DNA No translation available.
AC027801 Genomic DNA No translation available.
CH471109 Genomic DNA Translation: EAW94658.1
CH471109 Genomic DNA Translation: EAW94659.1
BC032640 mRNA Translation: AAH32640.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS11554.1 [O95251-1]
CCDS56035.1 [O95251-4]
CCDS56036.1 [O95251-2]
CCDS56037.1 [O95251-5]
CCDS56038.1 [O95251-3]

NCBI Reference Sequences

More...RefSeqi		NP_001186084.1, NM_001199155.1 [O95251-4]
NP_001186085.1, NM_001199156.1 [O95251-5]
NP_001186086.1, NM_001199157.1 [O95251-2]
NP_001186087.1, NM_001199158.1 [O95251-3]
NP_008998.1, NM_007067.4 [O95251-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000259021; ENSP00000259021; ENSG00000136504 [O95251-1]
ENST00000424009; ENSP00000398961; ENSG00000136504 [O95251-4]
ENST00000454930; ENSP00000413415; ENSG00000136504 [O95251-5]
ENST00000509773; ENSP00000424577; ENSG00000136504 [O95251-2]
ENST00000510819; ENSP00000423385; ENSG00000136504 [O95251-3]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		11143

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:11143

UCSC genome browser

More...UCSCi		uc002ipl.3, human [O95251-1]

Keywords - Coding sequence diversityi

Alternative splicing

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF074606 mRNA Translation: AAC99368.1
AF140360 mRNA Translation: AAD42348.1
AF217502 mRNA Translation: AAL56649.1
AK023890 mRNA Translation: BAG51236.1
AK293976 mRNA Translation: BAG57346.1
AK294014 mRNA Translation: BAG57375.1
AK294052 mRNA Translation: BAG57401.1
AK294836 mRNA Translation: BAG57945.1
AC015795 Genomic DNA No translation available.
AC027801 Genomic DNA No translation available.
CH471109 Genomic DNA Translation: EAW94658.1
CH471109 Genomic DNA Translation: EAW94659.1
BC032640 mRNA Translation: AAH32640.1
CCDSiCCDS11554.1 [O95251-1]
CCDS56035.1 [O95251-4]
CCDS56036.1 [O95251-2]
CCDS56037.1 [O95251-5]
CCDS56038.1 [O95251-3]
RefSeqiNP_001186084.1, NM_001199155.1 [O95251-4]
NP_001186085.1, NM_001199156.1 [O95251-5]
NP_001186086.1, NM_001199157.1 [O95251-2]
NP_001186087.1, NM_001199158.1 [O95251-3]
NP_008998.1, NM_007067.4 [O95251-1]

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
5GK9X-ray2.40A336-611[»]
6MAJX-ray2.14A336-609[»]
6MAKX-ray2.13A336-609[»]
SMRiO95251
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi116315, 87 interactors
ComplexPortaliCPX-718, HBO1-4.1 histone acetyltransferase complex
CPX-719, HBO1-4.2 histone acetyltransferase complex
CPX-720, HBO1-4.3 histone acetyltransferase complex
CPX-721, HBO1-5.1 histone acetyltransferase complex
CPX-722, HBO1-5.2 histone acetyltransferase complex
CPX-723, HBO1-5.3 histone acetyltransferase complex
CORUMiO95251
DIPiDIP-29697N
IntActiO95251, 62 interactors
MINTiO95251
STRINGi9606.ENSP00000259021

Chemistry databases

ChEMBLiCHEMBL3774299

PTM databases

iPTMnetiO95251
MetOSiteiO95251
PhosphoSitePlusiO95251
SwissPalmiO95251

Polymorphism and mutation databases

BioMutaiKAT7

Proteomic databases

EPDiO95251
jPOSTiO95251
MassIVEiO95251
MaxQBiO95251
PaxDbiO95251
PeptideAtlasiO95251
PRIDEiO95251
ProteomicsDBi17693
33968
50746 [O95251-1]
50747 [O95251-2]
50748 [O95251-3]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		17983, 354 antibodies

The DNASU plasmid repository

More...DNASUi		11143

Genome annotation databases

EnsembliENST00000259021; ENSP00000259021; ENSG00000136504 [O95251-1]
ENST00000424009; ENSP00000398961; ENSG00000136504 [O95251-4]
ENST00000454930; ENSP00000413415; ENSG00000136504 [O95251-5]
ENST00000509773; ENSP00000424577; ENSG00000136504 [O95251-2]
ENST00000510819; ENSP00000423385; ENSG00000136504 [O95251-3]
GeneIDi11143
KEGGihsa:11143
UCSCiuc002ipl.3, human [O95251-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		11143
DisGeNETi11143
EuPathDBiHostDB:ENSG00000136504.11

GeneCards: human genes, protein and diseases

More...GeneCardsi		KAT7
HGNCiHGNC:17016, KAT7
HPAiENSG00000136504, Low tissue specificity
MIMi609880, gene
neXtProtiNX_O95251
OpenTargetsiENSG00000136504
PharmGKBiPA134886407

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2747, Eukaryota
GeneTreeiENSGT00940000157744
HOGENOMiCLU_011815_6_1_1
InParanoidiO95251
OMAiXVRAQSR
OrthoDBi629545at2759
PhylomeDBiO95251
TreeFamiTF317619

Enzyme and pathway databases

PathwayCommonsiO95251
ReactomeiR-HSA-3214847, HATs acetylate histones
SIGNORiO95251

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		11143, 135 hits in 868 CRISPR screens

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

More...ChiTaRSi		KAT7, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		MYST2

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

More...GenomeRNAii		11143
PharosiO95251, Tbio

Protein Ontology

More...PROi		PR:O95251
RNActiO95251, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000136504, Expressed in testis and 234 other tissues
ExpressionAtlasiO95251, baseline and differential
GenevisibleiO95251, HS

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR016181, Acyl_CoA_acyltransferase
IPR002717, HAT_MYST-type
IPR036388, WH-like_DNA-bd_sf
IPR040706, Zf-MYST
IPR002515, Znf_C2H2C
IPR036060, Znf_C2H2C_sf
PfamiView protein in Pfam
PF01853, MOZ_SAS, 1 hit
PF01530, zf-C2HC, 1 hit
PF17772, zf-MYST, 1 hit
SUPFAMiSSF103637, SSF103637, 1 hit
SSF55729, SSF55729, 1 hit
PROSITEiView protein in PROSITE
PS51726, MYST_HAT, 1 hit
PS51802, ZF_CCHHC, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiKAT7_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: O95251
Secondary accession number(s): B3KN74
, B4DF85, B4DFB4, B4DFE0, B4DGY4, E7ER15, G5E9K7
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: May 1, 1999
Last modified: December 2, 2020
This is version 185 of the entry and version 1 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
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