Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q96T88 (UHRF1_HUMAN)

Entry version 178 (16 Oct 2019)
Sequence version 1 (01 Dec 2001)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

E3 ubiquitin-protein ligase UHRF1

Gene

UHRF1

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

Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. May be involved in DNA repair.9 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. EC:2.3.2.27

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei316Histone H3K4me01
Binding sitei327Histone H3R2me01
Binding sitei330Histone H3R2me01
Binding sitei469Methylcytosine1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei479Required to confer preferential recognition of cytosine over thymine1
Sitei489Required to discriminate between hemimethylated DNA versus symmetrically methylated DNA1
Sitei491Required for affinity and specificity for 5-mCpG sequence1

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 fingeri310 – 366PHD-typePROSITE-ProRule annotationAdd BLAST57
Zinc fingeri724 – 763RING-typePROSITE-ProRule annotationAdd BLAST40

<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 functionChromatin regulator, DNA-binding, Repressor, Transferase
Biological processCell cycle, DNA damage, DNA repair, Transcription, Transcription regulation, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-5334118 DNA methylation

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		Q96T88

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q96T88

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00143

<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:
E3 ubiquitin-protein ligase UHRF1 (EC:2.3.2.27)
Alternative name(s):
Inverted CCAAT box-binding protein of 90 kDa
Nuclear protein 95
Nuclear zinc finger protein Np95
Short name:
HuNp95
Short name:
hNp95
RING finger protein 106
RING-type E3 ubiquitin transferase UHRF1
Transcription factor ICBP90
Ubiquitin-like PHD and RING finger domain-containing protein 1
Short name:
hUHRF1
Ubiquitin-like-containing PHD and RING finger domains protein 1
<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:UHRF1
Synonyms:ICBP90, NP95, RNF106
<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 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_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 19

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:12556 UHRF1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		607990 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q96T88

<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

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

Defects in UHRF1 may be a cause of cancers. Overexpressed in many different forms of human cancers, including bladder, breast, cervical, colorectal and prostate cancers, as well as pancreatic adenocarcinomas, rhabdomyosarcomas and gliomas. Plays an important role in the correlation of histone modification and gene silencing in cancer progression. Expression is associated with a poor prognosis in patients with various cancers, suggesting that it participates in cancer progression.

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>Mutagenesisi142D → A: Impaired binding to histone H3 without affecting the protein folding; when associated with A-153. 1 Publication1
Mutagenesisi145D → A: Impaired binding to histone H3. 1 Publication1
Mutagenesisi152F → A: Impaired binding to histone H3. 1 Publication1
Mutagenesisi153E → A: Impaired binding to histone H3 without affecting the protein folding; when associated with A-142. 1 Publication1
Mutagenesisi188Y → A: Impaired binding to histone H3. 2 Publications1
Mutagenesisi190D → A: Slightly impaired binding to histone H3. 1 Publication1
Mutagenesisi191Y → A: Impaired binding to histone H3. 1 Publication1
Mutagenesisi295 – 296RR → AA: Disrupts the simultaneous binding to H3R2me0 and H3K9me3. 1 Publication2
Mutagenesisi298S → A: Diminishes phosphorylation by PKA. 1 Publication1
Mutagenesisi330Q → A or K: Does not affect ability to bind histone H3 peptide. 1 Publication1
Mutagenesisi334 – 335DE → AA: Abolishes binding to histone H3. 1 Publication2
Mutagenesisi334D → A: Impaired binding to histone H3. 3 Publications1
Mutagenesisi337D → A: Impaired binding to histone H3. 3 Publications1
Mutagenesisi433R → A: Does not affect ability to bind DNA. 1 Publication1
Mutagenesisi443R → A: Decreased ability to bind DNA. 1 Publication1
Mutagenesisi448G → D: Decreased affinity for DNA. 1 Publication1
Mutagenesisi466Y → G: Decreased ability to bind DNA. 1 Publication1
Mutagenesisi469D → G: Abolishes ability to bind hemimethylated DNA. 1
Mutagenesisi489N → A: Abolishes specificity to hemimethylated DNA. 1 Publication1
Mutagenesisi491R → A: Decreased binding to methylated DNA but does not affect ability to bind DNA. 2 Publications1
Mutagenesisi639S → A: Prevents phosphorylation by CDK1 during M phase, leading to increased stability. 1 Publication1
Mutagenesisi639S → D: Mimics phosphorylation; impaired interaction with USP7, leading to decreased stability. 1 Publication1
Mutagenesisi651S → A: No effect on in vitro phosphorylation by PKA. 1 Publication1
Mutagenesisi666S → A: No effect on in vitro phosphorylation by PKA. 1 Publication1
Mutagenesisi741H → A: Abolishes E3 ubiquitin-protein ligase activity. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		29128

Open Targets

More...OpenTargetsi		ENSG00000276043

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA37196

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q96T88

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2424510

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		UHRF1

Domain mapping of disease mutations (DMDM)

More...DMDMi		67462077

<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_00000561441 – 793E3 ubiquitin-protein ligase UHRF1Add BLAST793

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 residuei76PhosphoserineCombined sources1
Modified residuei91PhosphoserineCombined sources1
Modified residuei95PhosphoserineBy similarity1
Modified residuei165PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki279Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei287PhosphoserineCombined sources1
Modified residuei298Phosphoserine; by PKA2 Publications1
Modified residuei368PhosphoserineCombined sources1
Cross-linki385Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei399N6-acetyllysineCombined sources1
Modified residuei546N6-acetyllysine; alternateCombined sources1
Cross-linki546Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei639Phosphoserine; by CDK1Combined sources1 Publication1
Modified residuei651PhosphoserineCombined sources1
Cross-linki670Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei707PhosphoserineCombined sources1
Modified residuei709PhosphoserineCombined 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

Phosphorylation at Ser-298 of the linker region decreases the binding to H3K9me3. Phosphorylation at Ser-639 by CDK1 during M phase impairs interaction with USP7, preventing deubiquitination and leading to degradation by the proteasome.3 Publications
Ubiquitinated; which leads to proteasomal degradation. Autoubiquitinated; interaction with USP7 leads to deubiquitination and prevents degradation. Ubiquitination and degradation takes place during M phase, when phosphorylation at Ser-639 prevents interaction with USP7 and subsequent deubiquitination. Polyubiquitination may be stimulated by DNA damage.4 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q96T88

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q96T88

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q96T88

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q96T88

PeptideAtlas

More...PeptideAtlasi		Q96T88

PRoteomics IDEntifications database

More...PRIDEi		Q96T88

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		78215 [Q96T88-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q96T88

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

More...PhosphoSitePlusi		Q96T88

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q96T88

<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

Expressed in thymus, bone marrow, testis, lung and heart. Overexpressed in breast cancer.3 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed in fetal thymus, liver and kidney.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

Up-regulated in proliferating cells, and down-regulated in quiescent cells. Down-regulated upon adriamycin-induced DNA damage, in a p53/TP53 and CDKN1A-dependent way. Induced by E2F1 transcription factor.4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000276043 Expressed in 149 organ(s), highest expression level in oocyte

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q96T88 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q96T88 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA049408
HPA055446

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with DNMT3A and DNMT3B (By similarity).

Interacts with DNMT1; the interaction is direct.

Interacts with USP7; leading to its deubiquitination.

Interacts with histone H3.

Interacts with HDAC1, but not with HDAC2.

Interacts with UHRF1BP1.

Interacts with PML.

Interacts with EHMT2. Binds hemimethylated CpG containing oligonucleotides.

By similarity10 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

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		118893, 96 interactors

Protein interaction database and analysis system

More...IntActi		Q96T88, 30 interactors

Molecular INTeraction database

More...MINTi		Q96T88

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000479617

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q96T88

<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

1793
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		Q96T88

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q96T88

<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>Domaini1 – 78Ubiquitin-likePROSITE-ProRule annotationAdd BLAST78
Domaini419 – 582YDGPROSITE-ProRule annotationAdd BLAST164

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>Regioni133 – 209Tudor-like 1Add BLAST77
Regioni216 – 283Tudor-like 2Add BLAST68
Regioni296 – 301Linker6
Regioni333 – 337Histone H3R2me0 binding5
Regioni353 – 355Histone H3R2me0 binding3
Regioni445 – 446Required to promote base flippingBy similarity2
Regioni463 – 464Methylcytosine binding2
Regioni466 – 469Required for formation of a 5-methylcytosine-binding pocket4
Regioni478 – 481Required for formation of a 5-methylcytosine-binding pocket4

<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 tudor-like regions specifically recognize and bind histone H3 unmethylated at 'Arg-2' (H3R2me0), while the PHD-type zinc finger specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3). The tudor-like regions simultaneously recognizes H3K9me3 through a conserved aromatic cage in the first tudor-like subdomain and unmodified H3K4 (H3K4me0) within a groove between the tandem subdomains (PubMed:21489993, PubMed:21777816 and PubMed:22100450). The linker region plays a role in the formation of a histone H3-binding hole between the reader modules formed by the tudor-like regions and the PHD-type zinc finger by making extended contacts with the tandem tudor-like regions (PubMed:22837395).1 Publication
The YDG domain (also named SRA domain) specifically recognizes and binds hemimethylated DNA at replication forks (DNA that is only methylated on the mother strand of replicating DNA) (PubMed:17673620). It contains a binding pocket that accommodates the 5-methylcytosine that is flipped out of the duplex DNA. 2 specialized loops reach through the resulting gap in the DNA from both the major and the minor grooves to read the other 3 bases of the CpG duplex. The major groove loop confers both specificity for the CpG dinucleotide and discrimination against methylation of deoxycytidine of the complementary strand (PubMed:18772889). The YDG domain also recognizes and binds 5-hydroxymethylcytosine (5hmC) (PubMed:21731699).3 Publications
The RING finger is required for ubiquitin ligase activity.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri310 – 366PHD-typePROSITE-ProRule annotationAdd BLAST57
Zinc fingeri724 – 763RING-typePROSITE-ProRule annotationAdd BLAST40

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

Ensembl GeneTree

More...GeneTreei		ENSGT00390000008296

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000124662

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q96T88

KEGG Orthology (KO)

More...KOi		K10638

Database of Orthologous Groups

More...OrthoDBi		705927at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q96T88

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.30.280.10, 1 hit
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR015947 PUA-like_sf
IPR036987 SRA-YDG_sf
IPR003105 SRA_YDG
IPR021991 TTD_dom
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00628 PHD, 1 hit
PF02182 SAD_SRA, 1 hit
PF12148 TTD, 1 hit
PF00240 ubiquitin, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00249 PHD, 1 hit
SM00184 RING, 2 hits
SM00466 SRA, 1 hit
SM00213 UBQ, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF54236 SSF54236, 1 hit
SSF57903 SSF57903, 1 hit
SSF88697 SSF88697, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50053 UBIQUITIN_2, 1 hit
PS51015 YDG, 1 hit
PS01359 ZF_PHD_1, 1 hit
PS50016 ZF_PHD_2, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 2 hits

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

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

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q96T88-1) [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
MWIQVRTMDG RQTHTVDSLS RLTKVEELRR KIQELFHVEP GLQRLFYRGK 
        60         70         80         90        100
QMEDGHTLFD YEVRLNDTIQ LLVRQSLVLP HSTKERDSEL SDTDSGCCLG 
       110        120        130        140        150
QSESDKSSTH GEAAAETDSR PADEDMWDET ELGLYKVNEY VDARDTNMGA 
       160        170        180        190        200
WFEAQVVRVT RKAPSRDEPC SSTSRPALEE DVIYHVKYDD YPENGVVQMN 
       210        220        230        240        250
SRDVRARART IIKWQDLEVG QVVMLNYNPD NPKERGFWYD AEISRKRETR 
       260        270        280        290        300
TARELYANVV LGDDSLNDCR IIFVDEVFKI ERPGEGSPMV DNPMRRKSGP 
       310        320        330        340        350
SCKHCKDDVN RLCRVCACHL CGGRQDPDKQ LMCDECDMAF HIYCLDPPLS 
       360        370        380        390        400
SVPSEDEWYC PECRNDASEV VLAGERLRES KKKAKMASAT SSSQRDWGKG 
       410        420        430        440        450
MACVGRTKEC TIVPSNHYGP IPGIPVGTMW RFRVQVSESG VHRPHVAGIH 
       460        470        480        490        500
GRSNDGAYSL VLAGGYEDDV DHGNFFTYTG SGGRDLSGNK RTAEQSCDQK 
       510        520        530        540        550
LTNTNRALAL NCFAPINDQE GAEAKDWRSG KPVRVVRNVK GGKNSKYAPA 
       560        570        580        590        600
EGNRYDGIYK VVKYWPEKGK SGFLVWRYLL RRDDDEPGPW TKEGKDRIKK 
       610        620        630        640        650
LGLTMQYPEG YLEALANRER EKENSKREEE EQQEGGFASP RTGKGKWKRK 
       660        670        680        690        700
SAGGGPSRAG SPRRTSKKTK VEPYSLTAQQ SSLIREDKSN AKLWNEVLAS 
       710        720        730        740        750
LKDRPASGSP FQLFLSKVEE TFQCICCQEL VFRPITTVCQ HNVCKDCLDR 
       760        770        780        790 
SFRAQVFSCP ACRYDLGRSY AMQVNQPLQT VLNQLFPGYG NGR
Length:793
Mass (Da):89,814
Last modified:December 1, 2001 - 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:iE65B15657525C89F
GO
Isoform 2 (identifier: Q96T88-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGVFAVPPLSSDTM

Note: No experimental confirmation available.
Show »
Length:806
Mass (Da):91,116
Checksum:iBFE365939E846398
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
A0A087WVR3A0A087WVR3_HUMAN
E3 ubiquitin-protein ligase UHRF1
UHRF1 hCG_23497
806Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WTW0A0A087WTW0_HUMAN
E3 ubiquitin-protein ligase UHRF1
UHRF1
857Annotation 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>
A0A087WWG9A0A087WWG9_HUMAN
E3 ubiquitin-protein ligase UHRF1
UHRF1
496Annotation 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 BAB15177 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti383K → E in BAF82078 (PubMed:14702039).Curated1
Sequence conflicti383K → N in AAF28469 (PubMed:10646863).Curated1
Sequence conflicti457A → S in AAF28469 (PubMed:10646863).Curated1
Sequence conflicti675S → N in BAF82078 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022554240D → H1 PublicationCorresponds to variant dbSNP:rs17886098Ensembl.1
Natural variantiVAR_022555379E → K2 PublicationsCorresponds to variant dbSNP:rs17885791Ensembl.1
Natural variantiVAR_022556638A → T2 PublicationsCorresponds to variant dbSNP:rs2307209Ensembl.1
Natural variantiVAR_022557642T → M1 PublicationCorresponds to variant dbSNP:rs17884843Ensembl.1
Natural variantiVAR_022558713L → F1 PublicationCorresponds to variant dbSNP:rs17883563Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0443941M → MGVFAVPPLSSDTM in isoform 2. 1 Publication1

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
AF129507 mRNA Translation: AAF28469.1
AB177623 mRNA Translation: BAF36719.1
AB177624 mRNA Translation: BAF36720.1
AB075601 mRNA Translation: BAC20576.1
AF274048 mRNA Translation: AAK55744.1
EF560733 mRNA Translation: ABQ59043.1
AK025578 mRNA Translation: BAB15177.1 Different initiation.
AK289389 mRNA Translation: BAF82078.1
AK314579 mRNA Translation: BAG37156.1
AY787925 Genomic DNA Translation: AAV40831.1
AC027319 Genomic DNA No translation available.
AC053467 Genomic DNA Translation: AAF64067.1
CH471139 Genomic DNA Translation: EAW69187.1
BC113875 mRNA Translation: AAI13876.2

The Consensus CDS (CCDS) project

More...CCDSi		CCDS74262.1 [Q96T88-2]
CCDS74263.1 [Q96T88-1]

NCBI Reference Sequences

More...RefSeqi		NP_001041666.1, NM_001048201.2 [Q96T88-1]
NP_001276979.1, NM_001290050.1 [Q96T88-1]
NP_001276980.1, NM_001290051.1 [Q96T88-1]
NP_001276981.1, NM_001290052.1 [Q96T88-1]
NP_037414.3, NM_013282.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000612630; ENSP00000484739; ENSG00000276043 [Q96T88-1]
ENST00000615884; ENSP00000478601; ENSG00000276043 [Q96T88-1]
ENST00000616255; ENSP00000478348; ENSG00000276043 [Q96T88-1]
ENST00000624301; ENSP00000485604; ENSG00000276043 [Q96T88-1]
ENST00000650932; ENSP00000498698; ENSG00000276043 [Q96T88-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		29128

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:29128

UCSC genome browser

More...UCSCi		uc032hkj.2 human [Q96T88-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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

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

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

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF129507 mRNA Translation: AAF28469.1
AB177623 mRNA Translation: BAF36719.1
AB177624 mRNA Translation: BAF36720.1
AB075601 mRNA Translation: BAC20576.1
AF274048 mRNA Translation: AAK55744.1
EF560733 mRNA Translation: ABQ59043.1
AK025578 mRNA Translation: BAB15177.1 Different initiation.
AK289389 mRNA Translation: BAF82078.1
AK314579 mRNA Translation: BAG37156.1
AY787925 Genomic DNA Translation: AAV40831.1
AC027319 Genomic DNA No translation available.
AC053467 Genomic DNA Translation: AAF64067.1
CH471139 Genomic DNA Translation: EAW69187.1
BC113875 mRNA Translation: AAI13876.2
CCDSiCCDS74262.1 [Q96T88-2]
CCDS74263.1 [Q96T88-1]
RefSeqiNP_001041666.1, NM_001048201.2 [Q96T88-1]
NP_001276979.1, NM_001290050.1 [Q96T88-1]
NP_001276980.1, NM_001290051.1 [Q96T88-1]
NP_001276981.1, NM_001290052.1 [Q96T88-1]
NP_037414.3, NM_013282.4

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
2FAZX-ray2.00A/B1-76[»]
2L3RNMR-A126-285[»]
2LGGNMR-A298-366[»]
2LGKNMR-A298-366[»]
2LGLNMR-A298-366[»]
2PB7X-ray1.90A408-643[»]
3ASKX-ray2.90A/B/C/D134-367[»]
3ASLX-ray1.41A298-367[»]
3BI7X-ray1.70A414-617[»]
3CLZX-ray2.20A/B/C/D414-617[»]
3DB3X-ray2.40A126-285[»]
3DB4X-ray2.40A126-285[»]
3DWHX-ray1.95A414-617[»]
3FL2X-ray1.75A672-793[»]
3SHBX-ray1.80A298-366[»]
3SOUX-ray1.80A/B298-367[»]
3SOWX-ray1.95A/B298-367[»]
3SOXX-ray2.65A/B298-367[»]
3T6RX-ray1.95A/B299-364[»]
3ZVYX-ray1.95A/B296-367[»]
3ZVZX-ray1.45B314-367[»]
4GY5X-ray2.96A/B/C/D134-366[»]
4QQDX-ray2.28A/B126-285[»]
5C6DX-ray2.29C/D634-665[»]
5IAYNMR-A134-285[»]
B642-657[»]
5XPIX-ray2.20A127-283[»]
5YY9X-ray2.65A/B123-285[»]
5YYAX-ray1.70A123-285[»]
6B9MX-ray1.68D638-678[»]
SMRiQ96T88
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi118893, 96 interactors
IntActiQ96T88, 30 interactors
MINTiQ96T88
STRINGi9606.ENSP00000479617

Chemistry databases

BindingDBiQ96T88
ChEMBLiCHEMBL2424510

PTM databases

iPTMnetiQ96T88
PhosphoSitePlusiQ96T88
SwissPalmiQ96T88

Polymorphism and mutation databases

BioMutaiUHRF1
DMDMi67462077

Proteomic databases

EPDiQ96T88
jPOSTiQ96T88
MassIVEiQ96T88
MaxQBiQ96T88
PeptideAtlasiQ96T88
PRIDEiQ96T88
ProteomicsDBi78215 [Q96T88-1]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		29128

Genome annotation databases

EnsembliENST00000612630; ENSP00000484739; ENSG00000276043 [Q96T88-1]
ENST00000615884; ENSP00000478601; ENSG00000276043 [Q96T88-1]
ENST00000616255; ENSP00000478348; ENSG00000276043 [Q96T88-1]
ENST00000624301; ENSP00000485604; ENSG00000276043 [Q96T88-1]
ENST00000650932; ENSP00000498698; ENSG00000276043 [Q96T88-1]
GeneIDi29128
KEGGihsa:29128
UCSCiuc032hkj.2 human [Q96T88-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		29128
DisGeNETi29128

GeneCards: human genes, protein and diseases

More...GeneCardsi		UHRF1
HGNCiHGNC:12556 UHRF1
HPAiHPA049408
HPA055446
MIMi607990 gene
neXtProtiNX_Q96T88
OpenTargetsiENSG00000276043
PharmGKBiPA37196

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

GeneTreeiENSGT00390000008296
HOGENOMiHOG000124662
InParanoidiQ96T88
KOiK10638
OrthoDBi705927at2759
PhylomeDBiQ96T88

Enzyme and pathway databases

UniPathwayiUPA00143
ReactomeiR-HSA-5334118 DNA methylation
SignaLinkiQ96T88
SIGNORiQ96T88

Miscellaneous databases

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

More...ChiTaRSi		UHRF1 human
EvolutionaryTraceiQ96T88

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		UHRF1

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

More...GenomeRNAii		29128
PharosiQ96T88

Protein Ontology

More...PROi		PR:Q96T88

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000276043 Expressed in 149 organ(s), highest expression level in oocyte
ExpressionAtlasiQ96T88 baseline and differential
GenevisibleiQ96T88 HS

Family and domain databases

Gene3Di2.30.280.10, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR015947 PUA-like_sf
IPR036987 SRA-YDG_sf
IPR003105 SRA_YDG
IPR021991 TTD_dom
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PfamiView protein in Pfam
PF00628 PHD, 1 hit
PF02182 SAD_SRA, 1 hit
PF12148 TTD, 1 hit
PF00240 ubiquitin, 1 hit
SMARTiView protein in SMART
SM00249 PHD, 1 hit
SM00184 RING, 2 hits
SM00466 SRA, 1 hit
SM00213 UBQ, 1 hit
SUPFAMiSSF54236 SSF54236, 1 hit
SSF57903 SSF57903, 1 hit
SSF88697 SSF88697, 1 hit
PROSITEiView protein in PROSITE
PS50053 UBIQUITIN_2, 1 hit
PS51015 YDG, 1 hit
PS01359 ZF_PHD_1, 1 hit
PS50016 ZF_PHD_2, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 2 hits

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 nameiUHRF1_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: Q96T88
Secondary accession number(s): A0JBR2
, A8K024, B2RBA9, Q2HIX7, Q8J022, Q9H6S6, Q9P115, Q9P1U7
<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: June 7, 2005
Last sequence update: December 1, 2001
Last modified: October 16, 2019
This is version 178 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, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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