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 178 (18 Sep 2019)
Sequence version 2 (28 Nov 2012)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Zinc finger MYND domain-containing protein 11

Gene

ZMYND11

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

Chromatin reader that specifically recognizes and binds histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3) and regulates RNA polymerase II elongation. Does not bind other histone H3 subtypes (H3.1 or H3.2) (By similarity). Colocalizes with highly expressed genes and functions as a transcription corepressor by modulating RNA polymerase II at the elongation stage. Binds non-specifically to dsDNA (PubMed:24675531). Acts as a tumor-suppressor by repressing a transcriptional program essential for tumor cell growth.By similarity3 Publications
(Microbial infection) Inhibits Epstein-Barr virus EBNA2-mediated transcriptional activation and host cell proliferation, through direct interaction.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi258ZincCombined sources1 Publication1
Metal bindingi261ZincCombined sources1 Publication1
Metal bindingi277ZincCombined sources1 Publication1
Metal bindingi281Zinc; via tele nitrogenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri100 – 148PHD-typePROSITE-ProRule annotationAdd BLAST49
Zinc fingeri563 – 598MYND-typePROSITE-ProRule annotation1 PublicationAdd BLAST36

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

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

Molecular functionChromatin regulator, DNA-binding, Repressor
Biological processCell cycle, Host-virus interaction, Transcription, Transcription regulation
LigandMetal-binding, Zinc

<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:
Zinc finger MYND domain-containing protein 11Curated
Alternative name(s):
Adenovirus 5 E1A-binding protein
Bone morphogenetic protein receptor-associated molecule 1
Protein BS69
<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:ZMYND11Imported
Synonyms:BRAM1, BS691 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 10

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:16966 ZMYND11

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
608668 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q15326

<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

Chromosome, Nucleus

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

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

A chromosomal aberration involving ZMYND11 is a cause of acute poorly differentiated myeloid leukemia. Translocation (10;17)(p15;q21) with MBTD1.1 Publication
Mental retardation, autosomal dominant 30 (MRD30)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD30 patients manifest mild intellectual disability and subtle facial dysmorphisms, including hypertelorism, ptosis, and a wide mouth.
Related information in OMIM

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>Mutagenesisi258 – 261CKNC → AKNA: No effect on nuclear location. 1 Publication4
Mutagenesisi287K → A: Abolishes binding to DNA. No effect on nuclear location. 1 Publication1
Mutagenesisi289K → A: Abolishes binding to DNA. No effect on nuclear location. 1 Publication1
Mutagenesisi291F → A: No effect on nuclear location. 1 Publication1
Mutagenesisi294W → A: Abolishes interaction with Histone 3. Diffused distribution in the nucleus. 1 Publication1
Mutagenesisi310F → A: Diffused distribution in the nucleus. 1 Publication1
Mutagenesisi334R → A: Decreases binding to DNA. 1 Publication1
Mutagenesisi338 – 339KR → AA: No effect on interaction with Histone 3. Abolishes binding to DNA. Changes location from nuclear to cytoplasmic. 1 Publication2
Mutagenesisi344 – 345KK → AA: Abolishes binding to DNA. No effect on nuclear location. 1 Publication2
Mutagenesisi562W → Y: Reduced interaction with PXLXP ligand MGA without affecting interaction with viral human adenovirus early E1A protein. 1 Publication1
Mutagenesisi563C → S: Abrogates binding to EZH2. 1 Publication1
Mutagenesisi567 – 568EE → KK: Reduced interaction with PXLXP ligand proteins. 1 Publication2
Mutagenesisi572Y → A: Decreases interaction with Epstein-Barr virus EBNA2 protein. 1 Publication1
Mutagenesisi586Q → A: Highly decreases interaction with Epstein-Barr virus EBNA2 protein. No effect on the inhibition of EBNA2-mediated transcriptional activation. Almost abolishes interaction with Epstein-Barr virus EBNA2 protein and inhibition of EBNA2-mediated transcriptional activation; when associated with A-590. 1 Publication1
Mutagenesisi590W → A: Highly decreases interaction with Epstein-Barr virus EBNA2 protein. Almost abolishes interaction with Epstein-Barr virus EBNA2 protein and inhibition of EBNA2-mediated transcriptional activation; when associated with A-590. 1 Publication1
Mutagenesisi599 – 602RRKR → GGGG: Abolished interaction with PXLXP ligand proteins. 1 Publication4
Mutagenesisi600R → A: Highly decreases interaction with Epstein-Barr virus EBNA2 protein. 1 Publication1

Keywords - Diseasei

Mental retardation, Tumor suppressor

Organism-specific databases

DisGeNET

More...
DisGeNETi
10771

MalaCards human disease database

More...
MalaCardsi
ZMYND11
MIMi616083 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000015171

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

More...
Orphaneti
178469 Autosomal dominant non-syndromic intellectual disability

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA128394578

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ZMYND11

Domain mapping of disease mutations (DMDM)

More...
DMDMi
425906058

<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_00002112181 – 602Zinc finger MYND domain-containing protein 11Add BLAST602

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki366Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki407Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki408Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei421PhosphoserineCombined sources1

<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

Sumoylated following its interaction with PIAS1 and UBE2I.1 Publication
Ubiquitinated, leading to proteasomal degradation.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q15326

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q15326

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
Q15326

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

More...
PaxDbi
Q15326

PeptideAtlas

More...
PeptideAtlasi
Q15326

PRoteomics IDEntifications database

More...
PRIDEi
Q15326

ProteomicsDB human proteome resource

More...
ProteomicsDBi
28024
60529 [Q15326-1]
61337
6423

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q15326

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

More...
PhosphoSitePlusi
Q15326

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

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

Ubiquitous.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Down-regulated in breast cancer patients with poor prognosis.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000015171 Expressed in 252 organ(s), highest expression level in cauda epididymis

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q15326 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q15326 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA015816

<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

Homooligomer; forms homooligomers via its C-terminus (PubMed:26845565).

Interacts with histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3) (PubMed:24675531).

Interacts (via MYND-type zinc finger) with NCOR1 (PubMed:10734313).

Interacts (via MYND-type zinc finger) with MGA protein (via PXLXP motif) (PubMed:23372760).

Interacts (via MYND-type zinc finger) with EZH2 (PubMed:16565076).

Interacts with EMSY and E2F6 (PubMed:15947784, PubMed:16565076).

Interacts with PIAS1 and UBE2I (PubMed:19766626).

7 Publications

(Microbial infection)

Interacts (via MYND-type zinc finger) with human adenovirus early E1A protein (via PXLXP motif); this interaction inhibits E1A mediated transactivation.

2 Publications

(Microbial infection)

Interacts (via MYND-type zinc finger) with Epstein-Barr virus EBNA2 protein (via PXLXP motif) (PubMed:11733528, PubMed:26845565).

Interacts with Epstein-Barr virus-derived protein LMP1; leading to negatively regulate NF-kappa-B activation by Epstein-Barr virus-derived protein LMP1 (PubMed:12181323, PubMed:16382137, PubMed:19379743, PubMed:20138174).

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
115989, 61 interactors

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q15326

Protein interaction database and analysis system

More...
IntActi
Q15326, 27 interactors

Molecular INTeraction database

More...
MINTi
Q15326

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000381053

<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

1602
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
Q15326

Database of comparative protein structure models

More...
ModBasei
Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini168 – 238BromoPROSITE-ProRule annotationAdd BLAST71
Domaini280 – 331PWWPPROSITE-ProRule annotationAdd BLAST52

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>Regioni452 – 572Interaction with human adenovirus E1AAdd BLAST121

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi394 – 400Nuclear localization signalSequence analysis7

<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 PWWP domain specifically recognizes and binds histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3) and adopts a five-bladed beta-barrel fold with an extended C-terminal alpha-helix, with a conserved H3.3K36me3-binding aromatic cage formed by Phe-291 and Trp-294 of the beta1-beta2 loop and Phe-310 of the beta3-beta4 loop. Specific recognition of H3.3 histone is mediated by the encapsulation of the H3.3-specific 'Ser 31' residue in a composite pocket formed by the tandem bromo-PWWP domains.1 Publication

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri100 – 148PHD-typePROSITE-ProRule annotationAdd BLAST49
Zinc fingeri563 – 598MYND-typePROSITE-ProRule annotation1 PublicationAdd BLAST36

Keywords - Domaini

Bromodomain, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3612 Eukaryota
ENOG410XTCC LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156942

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000038026

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q15326

KEGG Orthology (KO)

More...
KOi
K23218

Identification of Orthologs from Complete Genome Data

More...
OMAi
NTSKQEM

Database of Orthologous Groups

More...
OrthoDBi
369818at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q15326

TreeFam database of animal gene trees

More...
TreeFami
TF106407

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05841 BS69_related, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.920.10, 1 hit
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001487 Bromodomain
IPR036427 Bromodomain-like_sf
IPR000313 PWWP_dom
IPR019786 Zinc_finger_PHD-type_CS
IPR035505 ZMYND8/11_PWWP
IPR011011 Znf_FYVE_PHD
IPR002893 Znf_MYND
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR013083 Znf_RING/FYVE/PHD

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00439 Bromodomain, 1 hit
PF00855 PWWP, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00297 BROMO, 1 hit
SM00249 PHD, 1 hit
SM00293 PWWP, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47370 SSF47370, 1 hit
SSF57903 SSF57903, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50014 BROMODOMAIN_2, 1 hit
PS50812 PWWP, 1 hit
PS01360 ZF_MYND_1, 1 hit
PS50865 ZF_MYND_2, 1 hit
PS01359 ZF_PHD_1, 1 hit
PS50016 ZF_PHD_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. 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 (6+)i

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

This entry describes 6 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 6 described isoforms and 7 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q15326-1) [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
MARLTKRRQA DTKAIQHLWA AIEIIRNQKQ IANIDRITKY MSRVHGMHPK
60 70 80 90 100
ETTRQLSLAV KDGLIVETLT VGCKGSKAGI EQEGYWLPGD EIDWETENHD
110 120 130 140 150
WYCFECHLPG EVLICDLCFR VYHSKCLSDE FRLRDSSSPW QCPVCRSIKK
160 170 180 190 200
KNTNKQEMGT YLRFIVSRMK ERAIDLNKKG KDNKHPMYRR LVHSAVDVPT
210 220 230 240 250
IQEKVNEGKY RSYEEFKADA QLLLHNTVIF YGADSEQADI ARMLYKDTCH
260 270 280 290 300
ELDELQLCKN CFYLSNARPD NWFCYPCIPN HELVWAKMKG FGFWPAKVMQ
310 320 330 340 350
KEDNQVDVRF FGHHHQRAWI PSENIQDITV NIHRLHVKRS MGWKKACDEL
360 370 380 390 400
ELHQRFLREG RFWKSKNEDR GEEEAESSIS STSNEQLKVT QEPRAKKGRR
410 420 430 440 450
NQSVEPKKEE PEPETEAVSS SQEIPTMPQP IEKVSVSTQT KKLSASSPRM
460 470 480 490 500
LHRSTQTTND GVCQSMCHDK YTKIFNDFKD RMKSDHKRET ERVVREALEK
510 520 530 540 550
LRSEMEEEKR QAVNKAVANM QGEMDRKCKQ VKEKCKEEFV EEIKKLATQH
560 570 580 590 600
KQLISQTKKK QWCYNCEEEA MYHCCWNTSY CSIKCQQEHW HAEHKRTCRR

KR
Length:602
Mass (Da):70,963
Last modified:November 28, 2012 - 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:i3AD525B90574BDE8
GO
Isoform 2 (identifier: Q15326-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     93-146: Missing.

Show »
Length:548
Mass (Da):64,426
Checksum:i5EDF3D170E2EDD11
GO
Isoform 3 (identifier: Q15326-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     563-602: CYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR → VNTSLF

Show »
Length:568
Mass (Da):66,590
Checksum:i597E186F867E225B
GO
Isoform 4 (identifier: Q15326-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     93-146: Missing.
     563-602: CYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR → VNTSLF

Show »
Length:514
Mass (Da):60,053
Checksum:iC20F5B606BAB0E2E
GO
Isoform 5 (identifier: Q15326-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     93-146: Missing.
     173-203: Missing.

Note: No experimental confirmation available.
Show »
Length:517
Mass (Da):60,869
Checksum:iE8EA00DD12FA4FF8
GO
Isoform 6 (identifier: Q15326-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     233-233: Missing.
     563-602: CYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR → VNTSLF

Note: No experimental confirmation available.
Show »
Length:567
Mass (Da):66,519
Checksum:i86FC85955F1022E5
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
J3QKD2J3QKD2_HUMAN
Zinc finger MYND domain-containing ...
ZMYND11 hCG_23206
585Annotation 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>
E7ENI9E7ENI9_HUMAN
Zinc finger MYND domain-containing ...
ZMYND11
571Annotation 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>
B0QZE2B0QZE2_HUMAN
Zinc finger MYND domain-containing ...
ZMYND11
522Annotation 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>
B7Z2J6B7Z2J6_HUMAN
Zinc finger MYND domain-containing ...
ZMYND11
547Annotation 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>
A0A0A0MRY2A0A0A0MRY2_HUMAN
Zinc finger MYND domain-containing ...
ZMYND11
482Annotation 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>
E7EV75E7EV75_HUMAN
Zinc finger MYND domain-containing ...
ZMYND11
213Annotation 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>
E9PE09E9PE09_HUMAN
Zinc finger MYND domain-containing ...
ZMYND11
140Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH34784 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG35465 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA60052 differs from that shown. Reason: Frameshift at positions 11 and 39.Curated

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_04448293 – 146Missing in isoform 2, isoform 4 and isoform 5. 2 PublicationsAdd BLAST54
Alternative sequenceiVSP_046246173 – 203Missing in isoform 5. 1 PublicationAdd BLAST31
Alternative sequenceiVSP_047209233Missing in isoform 6. 1 Publication1
Alternative sequenceiVSP_044483563 – 602CYNCE…CRRKR → VNTSLF in isoform 3, isoform 4 and isoform 6. 2 PublicationsAdd BLAST40

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
X86098 mRNA Translation: CAA60052.1 Frameshift.
DQ335452 mRNA Translation: ABC72408.1
DQ335453 mRNA Translation: ABC72409.1
DQ335454 mRNA Translation: ABC72410.1
DQ335455 mRNA Translation: ABC72411.1
AK294469 mRNA Translation: BAH11779.1
AK312570 mRNA Translation: BAG35465.1 Different initiation.
AL589988 Genomic DNA No translation available.
AL603831 Genomic DNA No translation available.
AL713922 Genomic DNA No translation available.
AL731539 Genomic DNA No translation available.
CH471072 Genomic DNA Translation: EAW86539.1
CH471072 Genomic DNA Translation: EAW86540.1
CH471072 Genomic DNA Translation: EAW86541.1
BC034784 mRNA Translation: AAH34784.1 Different initiation.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS55696.1 [Q15326-3]
CCDS55697.1 [Q15326-5]
CCDS7052.2 [Q15326-1]
CCDS7053.2 [Q15326-6]
CCDS73060.1 [Q15326-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
S56145

NCBI Reference Sequences

More...
RefSeqi
NP_001189393.1, NM_001202464.1 [Q15326-2]
NP_001189394.1, NM_001202465.1 [Q15326-5]
NP_001189396.1, NM_001202467.1 [Q15326-4]
NP_001189397.1, NM_001202468.1 [Q15326-3]
NP_006615.2, NM_006624.5 [Q15326-1]
NP_997644.2, NM_212479.3 [Q15326-6]
XP_005252416.1, XM_005252359.4
XP_005252418.1, XM_005252361.3
XP_005252419.1, XM_005252362.2
XP_006717439.1, XM_006717376.2
XP_016871076.1, XM_017015587.1 [Q15326-1]
XP_016871077.1, XM_017015588.1
XP_016871078.1, XM_017015589.1
XP_016871079.1, XM_017015590.1
XP_016871081.1, XM_017015592.1
XP_016871082.1, XM_017015593.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000381591; ENSP00000371003; ENSG00000015171 [Q15326-1]
ENST00000381607; ENSP00000371020; ENSG00000015171 [Q15326-2]
ENST00000397959; ENSP00000381050; ENSG00000015171 [Q15326-5]
ENST00000397962; ENSP00000381053; ENSG00000015171 [Q15326-1]
ENST00000509513; ENSP00000424205; ENSG00000015171 [Q15326-6]
ENST00000558098; ENSP00000452959; ENSG00000015171 [Q15326-3]
ENST00000602682; ENSP00000473321; ENSG00000015171 [Q15326-5]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
10771

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:10771

UCSC genome browser

More...
UCSCi
uc001ifk.4 human [Q15326-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86098 mRNA Translation: CAA60052.1 Frameshift.
DQ335452 mRNA Translation: ABC72408.1
DQ335453 mRNA Translation: ABC72409.1
DQ335454 mRNA Translation: ABC72410.1
DQ335455 mRNA Translation: ABC72411.1
AK294469 mRNA Translation: BAH11779.1
AK312570 mRNA Translation: BAG35465.1 Different initiation.
AL589988 Genomic DNA No translation available.
AL603831 Genomic DNA No translation available.
AL713922 Genomic DNA No translation available.
AL731539 Genomic DNA No translation available.
CH471072 Genomic DNA Translation: EAW86539.1
CH471072 Genomic DNA Translation: EAW86540.1
CH471072 Genomic DNA Translation: EAW86541.1
BC034784 mRNA Translation: AAH34784.1 Different initiation.
CCDSiCCDS55696.1 [Q15326-3]
CCDS55697.1 [Q15326-5]
CCDS7052.2 [Q15326-1]
CCDS7053.2 [Q15326-6]
CCDS73060.1 [Q15326-2]
PIRiS56145
RefSeqiNP_001189393.1, NM_001202464.1 [Q15326-2]
NP_001189394.1, NM_001202465.1 [Q15326-5]
NP_001189396.1, NM_001202467.1 [Q15326-4]
NP_001189397.1, NM_001202468.1 [Q15326-3]
NP_006615.2, NM_006624.5 [Q15326-1]
NP_997644.2, NM_212479.3 [Q15326-6]
XP_005252416.1, XM_005252359.4
XP_005252418.1, XM_005252361.3
XP_005252419.1, XM_005252362.2
XP_006717439.1, XM_006717376.2
XP_016871076.1, XM_017015587.1 [Q15326-1]
XP_016871077.1, XM_017015588.1
XP_016871078.1, XM_017015589.1
XP_016871079.1, XM_017015590.1
XP_016871081.1, XM_017015592.1
XP_016871082.1, XM_017015593.1

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
4NS5X-ray1.90A154-371[»]
5HDAX-ray2.39A/C480-602[»]
SMRiQ15326
ModBaseiSearch...

Protein-protein interaction databases

BioGridi115989, 61 interactors
ELMiQ15326
IntActiQ15326, 27 interactors
MINTiQ15326
STRINGi9606.ENSP00000381053

PTM databases

iPTMnetiQ15326
PhosphoSitePlusiQ15326

Polymorphism and mutation databases

BioMutaiZMYND11
DMDMi425906058

Proteomic databases

EPDiQ15326
jPOSTiQ15326
MassIVEiQ15326
PaxDbiQ15326
PeptideAtlasiQ15326
PRIDEiQ15326
ProteomicsDBi28024
60529 [Q15326-1]
61337
6423

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
10771
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381591; ENSP00000371003; ENSG00000015171 [Q15326-1]
ENST00000381607; ENSP00000371020; ENSG00000015171 [Q15326-2]
ENST00000397959; ENSP00000381050; ENSG00000015171 [Q15326-5]
ENST00000397962; ENSP00000381053; ENSG00000015171 [Q15326-1]
ENST00000509513; ENSP00000424205; ENSG00000015171 [Q15326-6]
ENST00000558098; ENSP00000452959; ENSG00000015171 [Q15326-3]
ENST00000602682; ENSP00000473321; ENSG00000015171 [Q15326-5]
GeneIDi10771
KEGGihsa:10771
UCSCiuc001ifk.4 human [Q15326-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10771
DisGeNETi10771

GeneCards: human genes, protein and diseases

More...
GeneCardsi
ZMYND11
HGNCiHGNC:16966 ZMYND11
HPAiHPA015816
MalaCardsiZMYND11
MIMi608668 gene
616083 phenotype
neXtProtiNX_Q15326
OpenTargetsiENSG00000015171
Orphaneti178469 Autosomal dominant non-syndromic intellectual disability
PharmGKBiPA128394578

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3612 Eukaryota
ENOG410XTCC LUCA
GeneTreeiENSGT00940000156942
HOGENOMiHOG000038026
InParanoidiQ15326
KOiK23218
OMAiNTSKQEM
OrthoDBi369818at2759
PhylomeDBiQ15326
TreeFamiTF106407

Miscellaneous databases

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

More...
ChiTaRSi
ZMYND11 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
ZMYND11

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

More...
GenomeRNAii
10771

Pharos

More...
Pharosi
Q15326

Protein Ontology

More...
PROi
PR:Q15326

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000015171 Expressed in 252 organ(s), highest expression level in cauda epididymis
ExpressionAtlasiQ15326 baseline and differential
GenevisibleiQ15326 HS

Family and domain databases

CDDicd05841 BS69_related, 1 hit
Gene3Di1.20.920.10, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR001487 Bromodomain
IPR036427 Bromodomain-like_sf
IPR000313 PWWP_dom
IPR019786 Zinc_finger_PHD-type_CS
IPR035505 ZMYND8/11_PWWP
IPR011011 Znf_FYVE_PHD
IPR002893 Znf_MYND
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF00439 Bromodomain, 1 hit
PF00855 PWWP, 1 hit
SMARTiView protein in SMART
SM00297 BROMO, 1 hit
SM00249 PHD, 1 hit
SM00293 PWWP, 1 hit
SUPFAMiSSF47370 SSF47370, 1 hit
SSF57903 SSF57903, 1 hit
PROSITEiView protein in PROSITE
PS50014 BROMODOMAIN_2, 1 hit
PS50812 PWWP, 1 hit
PS01360 ZF_MYND_1, 1 hit
PS50865 ZF_MYND_2, 1 hit
PS01359 ZF_PHD_1, 1 hit
PS50016 ZF_PHD_2, 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 nameiZMY11_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: Q15326
Secondary accession number(s): B2R6G8
, B7Z293, F6UH50, Q2LD45, Q2LD46, Q2LD47, Q2LD48, Q5VUI1, Q8N4B3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 28, 2012
Last modified: September 18, 2019
This is version 178 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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

Do not show this banner again