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UniProtKB - Q7YRZ8 (MDM2_FELCA)

Entry version 114 (10 Feb 2021)
Sequence version 1 (01 Oct 2003)
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Protein

E3 ubiquitin-protein ligase Mdm2

Gene

MDM2

Organism
Felis catus (Cat) (Felis silvestris catus)
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

E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome. Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation. Ubiquitinates DCX, leading to DCX degradation and reduction of the dendritic spine density of olfactory bulb granule cells. Ubiquitinates DLG4, leading to proteasomal degradation of DLG4 which is required for AMPA receptor endocytosis.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.By similarity EC:2.3.2.27

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 fingeri299 – 328RanBP2-typePROSITE-ProRule annotationAdd BLAST30
Zinc fingeri438 – 479RING-typePROSITE-ProRule annotationAdd BLAST42

<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 functionTransferase
Biological processUbl conjugation pathway
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%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 Mdm2 (EC:2.3.2.27By similarity)
Alternative name(s):
Double minute 2 protein
RING-type E3 ubiquitin transferase Mdm2Curated
p53-binding protein Mdm2
<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:MDM2
<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>OrganismiFelis catus (Cat) (Felis silvestris catus)
<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 identifieri9685 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Feliformia › Felidae › Felinae › Felis
<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
  • UP000011712 <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

<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

Cytoplasm, 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_00001573301 – 491E3 ubiquitin-protein ligase Mdm2Add BLAST491

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 residuei166Phosphoserine; by SGK1By similarity1
Modified residuei190PhosphoserineBy similarity1
Modified residuei240PhosphoserineBy similarity1
Modified residuei242PhosphoserineBy similarity1
Modified residuei246PhosphoserineBy similarity1
Modified residuei260PhosphoserineBy similarity1
Modified residuei262PhosphoserineBy similarity1
Modified residuei386Phosphoserine; by ATMBy similarity1
Modified residuei395Phosphoserine; by ATMBy similarity1
Modified residuei407Phosphoserine; by ATMBy similarity1
Modified residuei419Phosphothreonine; by ATMBy similarity1
Modified residuei429Phosphoserine; by ATMBy similarity1

<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 on Ser-166 by SGK1 activates ubiquitination of p53/TP53. Phosphorylated at multiple sites near the RING domain by ATM upon DNA damage; this prevents oligomerization and E3 ligase processivity and impedes constitutive p53/TP53 degradation (By similarity).By similarity
Autoubiquitination leads to proteasomal degradation; resulting in p53/TP53 activation it may be regulated by SFN. Also ubiquitinated by TRIM13. Deubiquitinated by USP2 leads to its accumulation and increases deubiquitination and degradation of p53/TP53. Deubiquitinated by USP7 leading to its stabilization.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		Q7YRZ8

<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 p53/TP53, TP73/p73, RBL5 and RP11. Binds specifically to RNA. Can interact with RB1, E1A-associated protein EP300 and the E2F1 transcription factor.

Forms a ternary complex with p53/TP53 and WWOX.

Interacts with CDKN2AIP, RFWD3, USP7, PYHIN1 and RBBP6.

Interacts with ARRB1 and ARRB2.

Interacts with PSMA3.

Found in a trimeric complex with MDM2, MDM4 and USP2.

Interacts with USP2 (via N-terminus and C-terminus).

Interacts with MDM4.

Part of a complex with MDM2, DAXX, RASSF1 and USP7.

Part of a complex with DAXX, MDM2 and USP7.

Interacts directly with DAXX and USP7.

Interacts (via C-terminus) with RASSF1 isoform A (via N-terminus); the interaction is independent of TP53.

Interacts with APEX1; leading to its ubiquitination and degradation.

Interacts with RYBP; this inhibits ubiquitination of TP53.

Identified in a complex with RYBP and p53/TP53. Also component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in regulating p53/TP53 stabilization and activity. Binds directly both p53/TP53 and TRIM28.

Component of the TRIM28/KAP1-ERBB4-MDM2 complex involved in connecting growth factor responses with DNA damage.

Interacts directly with both TRIM28 and ERBB4 in the complex.

Interacts with DYRK2.

Interacts with IGF1R.

Interacts with TRIM13; the interaction ubiquitinates MDM2 leading to its proteasomal degradation.

Interacts with SNAI1; this interaction promotes SNAI1 ubiquitination.

Interacts with NOTCH1 (via intracellular domain).

Interacts with FHIT.

Interacts with RFFL and RNF34; the interaction stabilizes MDM2.

Interacts with CDK5RAP3 and CDKN2A/ARF; form a ternary complex involved in regulation of p53/TP53.

Interacts with MTA1.

Interacts with AARB2.

Interacts with MTBP.

Interacts with PML.

Interacts with RPL11.

Interacts with TBRG1.

Interacts with the 5S RNP which is composed of the 5S RNA, RPL5 and RPL11; the interaction is direct occurs in the nucleoplasm and negatively regulates MDM2-mediated TP53 ubiquitination and degradation.

Interacts with ADGRB1; the interaction results in inhibition of MDM2-mediated ubiquitination and degradation of DLG4/PSD95, promoting DLG4 stability and regulating synaptic plasticity.

Interacts with RPL23A; this interaction may promote p53/TP53 polyubiquitination (By similarity).

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		9685.ENSFCAP00000025067

<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

1491
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		Q7YRZ8

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

More...SMRi		Q7YRZ8

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini26 – 109SWIB/MDM2PROSITE-ProRule annotationAdd BLAST84

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 110Necessary for interaction with USP2By similarityAdd BLAST110
Regioni150 – 230Interaction with PYHIN1 and necessary for interaction with RFFL and RNF34By similarityAdd BLAST81
Regioni170 – 306Interaction with MTBPBy similarityAdd BLAST137
Regioni210 – 304ARF-bindingAdd BLAST95
Regioni223 – 232Interaction with USP7By similarity10
Regioni242 – 331Region IIAdd BLAST90
Regioni276 – 491Necessary for interaction with USP2By similarityAdd BLAST216

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>Motifi179 – 185Nuclear localization signalSequence analysis7
Motifi190 – 202Nuclear export signalAdd BLAST13
Motifi466 – 473Nucleolar localization signalSequence analysis8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi210 – 215Poly-Ser6
Compositional biasi243 – 301Asp/Glu-rich (acidic)Add BLAST59

<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

Region I is sufficient for binding p53 and inhibiting its G1 arrest and apoptosis functions. It also binds p73 and E2F1. Region II contains most of a central acidic region required for interaction with ribosomal protein L5 and a putative C4-type zinc finger. The RING finger domain which coordinates two molecules of zinc interacts specifically with RNA whether or not zinc is present and mediates the heterooligomerization with MDM4. It is also essential for its ubiquitin ligase E3 activity toward p53 and itself (By similarity).By similarity

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

Belongs to the MDM2/MDM4 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri299 – 328RanBP2-typePROSITE-ProRule annotationAdd BLAST30
Zinc fingeri438 – 479RING-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QQNV, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q7YRZ8

Database of Orthologous Groups

More...OrthoDBi		1329283at2759

Family and domain databases

Conserved Domains Database

More...CDDi		cd16783, mRING-HC-C2H2C4_MDM2, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.245.10, 1 hit
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR028340, Mdm2
IPR015459, MDM2_E3_ligase
IPR044080, MDM2_mRING-HC-C2H2C4
IPR016495, p53_neg-reg_MDM_2/4
IPR036885, SWIB_MDM2_dom_sf
IPR003121, SWIB_MDM2_domain
IPR001876, Znf_RanBP2
IPR036443, Znf_RanBP2_sf
IPR001841, Znf_RING
IPR013083, Znf_RING/FYVE/PHD

The PANTHER Classification System

More...PANTHERi		PTHR13844:SF15, PTHR13844:SF15, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02201, SWIB, 1 hit
PF00641, zf-RanBP, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF500700, MDM2, 1 hit
PIRSF006748, p53_MDM_2/4, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47592, SSF47592, 2 hits
SSF90209, SSF90209, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51925, SWIB_MDM2, 1 hit
PS01358, ZF_RANBP2_1, 1 hit
PS50199, ZF_RANBP2_2, 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>Sequencei

<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.

Q7YRZ8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MCNTNMSVST DGAVSTSQMP ASEQETLVRP KPLLLKLLKS VGAQKDTYTM 
        60         70         80         90        100
KEVIFYLGQY IMTKRLYDEK QQHIVYCSND LLGDLFGVPS FSVKEHRKIY 
       110        120        130        140        150
TMIYRNLVVV NQHEPSDSGT SVSENRCHLE GGSDQKDPVQ ELQEEKPSSS 
       160        170        180        190        200
DLVSRPSTSS RRRTISETEE HSDELPGERQ RKRHKSDSIS LSFDESLALC 
       210        220        230        240        250
VIREICCERS SSSESTGTPS NPDLDAGVSE HSGDWLDQDS VSDQFSVEFE 
       260        270        280        290        300
VESLDSEDYS LSEEGQELSD EDDEVYRVTV YQAGESDTDS FEEDPEISLA 
       310        320        330        340        350
DYWKCTSCNE MNPPLPPHCN RCWALRENWL PEDKGKDKGK MPEKAKVENS 
       360        370        380        390        400
TQVEEGFDVP DCKRTTVNDS RESCAEENDD KITQASQSQE SEDYSQPSTS 
       410        420        430        440        450
NSIIHSSQED VKEFEREETQ DKEEIVEPSF PHNAIEPCVI CQGRPKNGCI 
       460        470        480        490 
VHGKTGHLMA CFTCAKKLKK RNKPCPVCRQ PIQMIVLTYF P
Length:491
Mass (Da):55,433
Last modified:October 1, 2003 - 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:iD93E25D638E88934
GO

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
AB099709 mRNA Translation: BAC78209.1

NCBI Reference Sequences

More...RefSeqi		NP_001009346.1, NM_001009346.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		493939

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		fca:493939

<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
AB099709 mRNA Translation: BAC78209.1
RefSeqiNP_001009346.1, NM_001009346.1

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
6SQSX-ray1.83A/D428-491[»]
BMRBiQ7YRZ8
SMRiQ7YRZ8
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000025067

Proteomic databases

PRIDEiQ7YRZ8

Genome annotation databases

GeneIDi493939
KEGGifca:493939

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4193

Phylogenomic databases

eggNOGiENOG502QQNV, Eukaryota
InParanoidiQ7YRZ8
OrthoDBi1329283at2759

Family and domain databases

CDDicd16783, mRING-HC-C2H2C4_MDM2, 1 hit
Gene3Di1.10.245.10, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR028340, Mdm2
IPR015459, MDM2_E3_ligase
IPR044080, MDM2_mRING-HC-C2H2C4
IPR016495, p53_neg-reg_MDM_2/4
IPR036885, SWIB_MDM2_dom_sf
IPR003121, SWIB_MDM2_domain
IPR001876, Znf_RanBP2
IPR036443, Znf_RanBP2_sf
IPR001841, Znf_RING
IPR013083, Znf_RING/FYVE/PHD
PANTHERiPTHR13844:SF15, PTHR13844:SF15, 1 hit
PfamiView protein in Pfam
PF02201, SWIB, 1 hit
PF00641, zf-RanBP, 1 hit
PIRSFiPIRSF500700, MDM2, 1 hit
PIRSF006748, p53_MDM_2/4, 1 hit
SUPFAMiSSF47592, SSF47592, 2 hits
SSF90209, SSF90209, 1 hit
PROSITEiView protein in PROSITE
PS51925, SWIB_MDM2, 1 hit
PS01358, ZF_RANBP2_1, 1 hit
PS50199, ZF_RANBP2_2, 1 hit
PS50089, ZF_RING_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 nameiMDM2_FELCA
<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: Q7YRZ8
<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: November 23, 2004
Last sequence update: October 1, 2003
Last modified: February 10, 2021
This is version 114 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

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

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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