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Entry version 125 (26 Feb 2020)
Sequence version 2 (07 Jun 2005)
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Protein

E3 ubiquitin-protein ligase UHRF1

Gene

Uhrf1

Organism
Rattus norvegicus (Rat)
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 (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • 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%5Fsection">'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%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei313Histone H3K4me0By similarity1
Binding sitei324Histone H3R2me0By similarity1
Binding sitei327Histone H3R2me0By similarity1
Binding sitei466MethylcytosineBy similarity1
<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>Sitei476Required to confer preferential recognition of cytosine over thymineBy similarity1
Sitei486Required to discriminate between hemimethylated DNA versus symmetrically methylated DNABy similarity1
Sitei488Required for affinity and specificity for 5-mCpG sequenceBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri296 – 363PHD-typePROSITE-ProRule annotationAdd BLAST68
Zinc fingeri705 – 744RING-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

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

Enzyme and pathway databases

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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
E3 ubiquitin-protein ligase UHRF1 (EC:2.3.2.27)
Alternative name(s):
Liver regeneration-related protein LRRG126
RING-type E3 ubiquitin transferase UHRF1
Ubiquitin-like PHD and RING finger domain-containing protein 1
Ubiquitin-like-containing PHD and RING finger domains protein 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Uhrf1
ORF Names:Ac2-121
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
1595855 Uhrf1

<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 describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000561461 – 774E3 ubiquitin-protein ligase UHRF1Add BLAST774

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 residuei76PhosphoserineBy similarity1
Modified residuei91PhosphoserineCombined sources1
Modified residuei93PhosphoserineCombined sources1
Modified residuei95PhosphoserineCombined sources1
Modified residuei161PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki276Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei284PhosphoserineCombined sources1
Modified residuei295Phosphoserine; by PKABy similarity1
Modified residuei365PhosphoserineBy similarity1
Cross-linki382Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei396N6-acetyllysineBy similarity1
Modified residuei511PhosphoserineBy similarity1
Modified residuei542N6-acetyllysine; alternateBy similarity1
Cross-linki542Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei631Phosphoserine; by CDK1By similarity1
Modified residuei641PhosphoserineBy similarity1
Modified residuei648PhosphoserineBy similarity1
Cross-linki656Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei751PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation at Ser-295 of the linker region decreases the binding to H3K9me3. Phosphorylation at Ser-631 by CDK1 during M phase impairs interaction with USP7, preventing deubiquitination and leading to degradation by the proteasome (By similarity).By similarity
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-631 prevents interaction with USP7 and subsequent deubiquitination. Polyubiquitination may be stimulated by DNA damage (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q7TPK1

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

More...
PaxDbi
Q7TPK1

PRoteomics IDEntifications database

More...
PRIDEi
Q7TPK1

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q7TPK1

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

More...
PhosphoSitePlusi
Q7TPK1

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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with DNMT3A and DNMT3B.

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 methylated CpG containing oligonucleotides (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000066794

<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

3D structure databases

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

More...
SMRi
Q7TPK1

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%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 78Ubiquitin-likePROSITE-ProRule annotationAdd BLAST78
Domaini416 – 578YDGPROSITE-ProRule annotationAdd BLAST163

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>Regioni129 – 205Tudor-like 1Add BLAST77
Regioni212 – 280Tudor-like 2Add BLAST69
Regioni293 – 298LinkerBy similarity6
Regioni330 – 334Histone H3R2me0 bindingBy similarity5
Regioni350 – 352Histone H3R2me0 bindingBy similarity3
Regioni382 – 605Methyl-CpG binding and interaction with HDAC1By similarityAdd BLAST224
Regioni442 – 443Required to promote base flippingBy similarity2
Regioni460 – 461Methylcytosine bindingBy similarity2
Regioni463 – 466Required for formation of a 5-methylcytosine-binding pocketBy similarity4
Regioni475 – 478Required for formation of a 5-methylcytosine-binding pocketBy similarity4

<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. 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 (By similarity).By similarity
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). 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. The YDG domain also recognizes and binds 5-hydroxymethylcytosine (5hmC) (By similarity).By similarity
The RING finger is required for ubiquitin ligase activity.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri296 – 363PHD-typePROSITE-ProRule annotationAdd BLAST68
Zinc fingeri705 – 744RING-typePROSITE-ProRule annotationAdd BLAST40

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IFAP Eukaryota
COG3440 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q7TPK1

KEGG Orthology (KO)

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KOi
K10638

Database of Orthologous Groups

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OrthoDBi
705927at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q7TPK1

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
IPR000626 Ubiquitin-like_dom
IPR029071 Ubiquitin-like_domsf
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, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

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

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q7TPK1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MWIQVRTMDG KETHTVNSLS RLTKVQELRK KIEELFHVEP QLQRLFYRGK
60 70 80 90 100
QMEDGHTLFD YDVRLNDTIQ LLVRQSLALP LSTKERDSEL SDSDSGYGVG
110 120 130 140 150
HSESDKSSTH GEGTADGDDK TVWEDTDLGL YKVNEYVDVR DNIFGAWFEA
160 170 180 190 200
QVVQVQKKAL SEEEPCSSSA IMAPEDDIMY HIKYDDYPEH GVDIVKAKNV
210 220 230 240 250
RARARTVIPW EDLEVGQVVM ANYNVDYPRK RGFWYDVEIC RKRQTRTARE
260 270 280 290 300
LYGNVMLLND SQLNNCRIIF VDEVLKIELP NERSPLIGSP SRRKSGPSCQ
310 320 330 340 350
YCKDDENKPC RKCACHICGG REAPEKQVLC DECDMAFHLY CLQPPLTCVP
360 370 380 390 400
PEPEWYCPSC RTDSSEVVQA GEKLKKSKKK AKMASATSSS RRDWGKGMAC
410 420 430 440 450
VGRTTECTIV PANHFGPIPG VPVGTMWRFR VQVSESGVHR PHVAGIHGRS
460 470 480 490 500
NDGAYSLVLA GGYEDDVDNG NFFTYTGSGG RDLSGNKRTA GQSSDQKLTN
510 520 530 540 550
NNRALALNCH SPINEKGAEA EDWRQGKPVR VVRNMKGGKH SKYAPAEGNR
560 570 580 590 600
YDGIYKVVKY WPEKGKSGFI VWRYLLRRDD TEPEPWTREG KDRTRQLGLT
610 620 630 640 650
MQYPEGYLEA LANKEKNRKR PAKALEQGPS SSKIGKSKRK STGPATTSPR
660 670 680 690 700
VSKKSKLEPY TLPLQQANLI KEDKGNAKLW DDVLSSLQDG PYQIFLSKVK
710 720 730 740 750
EAFQCICCQE LVFRPVTTVC QHNVCKDCLD RSFRAQVFSC PACRYDLDHS
760 770
SPTRVNQPLQ TILNQLFPGY GSGR
Length:774
Mass (Da):87,449
Last modified:June 7, 2005 - 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:iC2FB3112F2D2EF9E
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2JT07A0A0G2JT07_RAT
E3 ubiquitin-protein ligase UHRF1
Uhrf1
829Annotation 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>
A0A0G2JXJ2A0A0G2JXJ2_RAT
E3 ubiquitin-protein ligase UHRF1
Uhrf1
782Annotation 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 AAP86266 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AY321334 mRNA Translation: AAP86266.1 Different initiation.
BC099224 mRNA Translation: AAH99224.1

NCBI Reference Sequences

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RefSeqi
NP_001008882.1, NM_001008882.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
316129

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:316129

<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
AY321334 mRNA Translation: AAP86266.1 Different initiation.
BC099224 mRNA Translation: AAH99224.1
RefSeqiNP_001008882.1, NM_001008882.1

3D structure databases

SMRiQ7TPK1
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000066794

PTM databases

iPTMnetiQ7TPK1
PhosphoSitePlusiQ7TPK1

Proteomic databases

jPOSTiQ7TPK1
PaxDbiQ7TPK1
PRIDEiQ7TPK1

Genome annotation databases

GeneIDi316129
KEGGirno:316129

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
29128
RGDi1595855 Uhrf1

Phylogenomic databases

eggNOGiENOG410IFAP Eukaryota
COG3440 LUCA
InParanoidiQ7TPK1
KOiK10638
OrthoDBi705927at2759
PhylomeDBiQ7TPK1

Enzyme and pathway databases

UniPathwayiUPA00143

Miscellaneous databases

Protein Ontology

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PROi
PR:Q7TPK1

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
IPR000626 Ubiquitin-like_dom
IPR029071 Ubiquitin-like_domsf
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, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_RAT
<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: Q7TPK1
Secondary accession number(s): Q4FZR4
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: February 26, 2020
This is version 125 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

<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

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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