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Protein

M-phase inducer phosphatase 1

Gene

CDC25A

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

Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro.

<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

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Stimulated by B-type cyclins. Stimulated by PIM1-mediated phosphorylation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei4311

<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

  • chaperone binding Source: UniProtKB
  • phosphoprotein phosphatase activity Source: Reactome
  • protein kinase binding Source: UniProtKB
  • protein tyrosine phosphatase activity Source: GO_Central

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 functionHydrolase, Protein phosphatase
Biological processCell cycle, Cell division, Mitosis

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.3.48 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1362277 Transcription of E2F targets under negative control by DREAM complex
R-HSA-156711 Polo-like kinase mediated events
R-HSA-176187 Activation of ATR in response to replication stress
R-HSA-5689880 Ub-specific processing proteases
R-HSA-69202 Cyclin E associated events during G1/S transition
R-HSA-69273 Cyclin A/B1/B2 associated events during G2/M transition
R-HSA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry
R-HSA-8862803 Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P30304

<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:
M-phase inducer phosphatase 1 (EC:3.1.3.48)
Alternative name(s):
Dual specificity phosphatase Cdc25A
<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:CDC25A
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000164045.11

Human Gene Nomenclature Database

More...
HGNCi
HGNC:1725 CDC25A

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
116947 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P30304

<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; Source: COMPARTMENTS

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_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>Mutagenesisi76S → A: Abolishes ubiquitination and impairs CHEK1-dependent degradation following checkpoint activation. 2 Publications1
Mutagenesisi79S → A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. 1 Publication1
Mutagenesisi81D → A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. 1 Publication1
Mutagenesisi82S → A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. 1 Publication1
Mutagenesisi124S → A: Abrogates phosphorylation by CHEK2 and infrared-induced degradation. Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-178; A-279 and A-293. 4 Publications1
Mutagenesisi141 – 143KEN → AAA: Prevents ubiquitination and subsequent degradation by the APC/C ubiquitin ligase complex. 1 Publication3
Mutagenesisi178S → A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-279 and A-293. Abrogates 14-3-3 protein binding. 3 Publications1
Mutagenesisi279S → A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-293. 1 Publication1
Mutagenesisi293S → A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-279. 1 Publication1
Mutagenesisi431C → S: Abolishes phosphatase activity. 2 Publications1
Mutagenesisi507T → A: Abrogates 14-3-3 protein binding; increases binding to cyclin B1. 1 Publication1
Mutagenesisi513S → A: Increased stability following IR treatment. 1 Publication1
Mutagenesisi513S → D: Mimicks phosphorylation state, leading to promote degradation following IR treatment. 1 Publication1
Mutagenesisi514K → L: Abrogates binding to CCNB1; when associated with L-520. 1 Publication1
Mutagenesisi519S → A: Increased stability following IR treatment. 1 Publication1
Mutagenesisi519S → D: Mimicks phosphorylation state, leading to promote degradation following IR treatment. 1 Publication1
Mutagenesisi520R → L: Abrogates binding to CCNB1; when associated with L-514. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
993

Open Targets

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OpenTargetsi
ENSG00000164045

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA26259

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3775

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CDC25A

Domain mapping of disease mutations (DMDM)

More...
DMDMi
50403734

<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_00001986411 – 524M-phase inducer phosphatase 1Add BLAST524

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 residuei76Phosphoserine; by CHEK12 Publications1
Modified residuei79Phosphoserine; by NEK111 Publication1
Modified residuei82Phosphoserine; by NEK112 Publications1
Modified residuei88Phosphoserine; by NEK112 Publications1
Modified residuei107PhosphoserineCombined sources1
Modified residuei124Phosphoserine; by CHEK1 and CHEK25 Publications1
Modified residuei178Phosphoserine; by CHEK13 Publications1
Modified residuei279Phosphoserine; by CHEK1 and CHEK21 Publication1
Modified residuei293Phosphoserine; by CHEK1 and CHEK21 Publication1
Modified residuei321PhosphoserineCombined sources1
Modified residuei507Phosphothreonine; by CHEK11 Publication1
Modified residuei513Phosphoserine; by PLK31 Publication1
Modified residuei519Phosphoserine; by PLK31 Publication1

<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

Phosphorylated by CHEK1 on Ser-76, Ser-124, Ser-178, Ser-279, Ser-293 and Thr-507 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-124, Ser-279, and Ser-293 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-178 and Thr-507 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-76, Ser-124, Ser-178, Ser-279 and Ser-293 may also promote ubiquitin-dependent proteolysis of CDC25A by the SCF complex. Phosphorylation of CDC25A at Ser-76 by CHEK1 primes it for subsequent phosphorylation at Ser-79, Ser-82 and Ser-88 by NEK11. Phosphorylation by NEK11 is required for BTRC-mediated polyubiquitination and degradation. Phosphorylation by PIM1 leads to an increase in phosphatase activity. Phosphorylated by PLK3 following DNA damage, leading to promote its ubiquitination and degradation.11 Publications
Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex that contains FZR1/CDH1 during G1 phase leading to its degradation by the proteasome. Ubiquitinated by a SCF complex containing BTRC and FBXW11 during S phase leading to its degradation by the proteasome. Deubiquitination by USP17L2/DUB3 leads to its stabilization.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P30304

MaxQB - The MaxQuant DataBase

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MaxQBi
P30304

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

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PaxDbi
P30304

PeptideAtlas

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PeptideAtlasi
P30304

PRoteomics IDEntifications database

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PRIDEi
P30304

ProteomicsDB human proteome resource

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ProteomicsDBi
54652
54653 [P30304-2]

PTM databases

DEPOD human dephosphorylation database

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DEPODi
P30304

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P30304

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

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PhosphoSitePlusi
P30304

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000164045 Expressed in 128 organ(s), highest expression level in secondary oocyte

CleanEx database of gene expression profiles

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CleanExi
HS_CDC25A

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P30304 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P30304 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA005855

<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 CCNB1/cyclin B1. Interacts with YWHAE/14-3-3 epsilon when phosphorylated. Interacts with CUL1 specifically when CUL1 is neddylated and active. Interacts with BTRC/BTRCP1 and FBXW11/BTRCP2. Interactions with CUL1, BTRC and FBXW11 are enhanced upon DNA damage. Interacts with PIM1. Interacts with CHEK2; mediates CDC25A phosphorylation and degradation in response to infrared-induced DNA damages. Interacts with HSP90AB1; prevents heat shock-mediated CDC25A degradation and contributes to cell cycle progression (PubMed:22843495).5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
107428, 80 interactors

Database of interacting proteins

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DIPi
DIP-166N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P30304

Protein interaction database and analysis system

More...
IntActi
P30304, 44 interactors

Molecular INTeraction database

More...
MINTi
P30304

STRING: functional protein association networks

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STRINGi
9606.ENSP00000303706

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P30304

<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

1524
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P30304

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

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SMRi
P30304

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P30304

<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>Domaini376 – 482RhodanesePROSITE-ProRule annotationAdd BLAST107

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>Motifi74 – 84PhosphodegronAdd BLAST11
Motifi141 – 143KEN box3

<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 phosphodegron motif mediates interaction with specific F-box proteins when phosphorylated. Putative phosphorylation sites at Ser-79 and Ser-82 appear to be essential for this interaction.1 Publication

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

Belongs to the MPI phosphatase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3772 Eukaryota
COG5105 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000160737

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000082672

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG052501

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P30304

KEGG Orthology (KO)

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KOi
K06645

Identification of Orthologs from Complete Genome Data

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OMAi
PQSYRPM

Database of Orthologous Groups

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OrthoDBi
EOG091G0H0D

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P30304

TreeFam database of animal gene trees

More...
TreeFami
TF101056

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01530 Cdc25, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.250.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000751 MPI_Phosphatase
IPR001763 Rhodanese-like_dom
IPR036873 Rhodanese-like_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF06617 M-inducer_phosp, 1 hit
PF00581 Rhodanese, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00716 MPIPHPHTASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00450 RHOD, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52821 SSF52821, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50206 RHODANESE_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P30304-1) [UniParc]FASTAAdd to basket
Also known as: CDC25A1

This isoform has been chosen as the 'canonical' 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
MELGPEPPHR RRLLFACSPP PASQPVVKAL FGASAAGGLS PVTNLTVTMD
60 70 80 90 100
QLQGLGSDYE QPLEVKNNSN LQRMGSSEST DSGFCLDSPG PLDSKENLEN
110 120 130 140 150
PMRRIHSLPQ KLLGCSPALK RSHSDSLDHD IFQLIDPDEN KENEAFEFKK
160 170 180 190 200
PVRPVSRGCL HSHGLQEGKD LFTQRQNSAP ARMLSSNERD SSEPGNFIPL
210 220 230 240 250
FTPQSPVTAT LSDEDDGFVD LLDGENLKNE EETPSCMASL WTAPLVMRTT
260 270 280 290 300
NLDNRCKLFD SPSLCSSSTR SVLKRPERSQ EESPPGSTKR RKSMSGASPK
310 320 330 340 350
ESTNPEKAHE TLHQSLSLAS SPKGTIENIL DNDPRDLIGD FSKGYLFHTV
360 370 380 390 400
AGKHQDLKYI SPEIMASVLN GKFANLIKEF VIIDCRYPYE YEGGHIKGAV
410 420 430 440 450
NLHMEEEVED FLLKKPIVPT DGKRVIVVFH CEFSSERGPR MCRYVRERDR
460 470 480 490 500
LGNEYPKLHY PELYVLKGGY KEFFMKCQSY CEPPSYRPMH HEDFKEDLKK
510 520
FRTKSRTWAG EKSKREMYSR LKKL
Length:524
Mass (Da):59,087
Last modified:July 19, 2004 - 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:iB2F6B792D4E6122B
GO
Isoform 2 (identifier: P30304-2) [UniParc]FASTAAdd to basket
Also known as: CDC25A2

The sequence of this isoform differs from the canonical sequence as follows:
     144-183: Missing.

Show »
Length:484
Mass (Da):54,551
Checksum:iAE6326F34B704D4B
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
C9JFR5C9JFR5_HUMAN
M-phase inducer phosphatase 1
CDC25A
252Annotation 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>
C9JH94C9JH94_HUMAN
M-phase inducer phosphatase 1
CDC25A
143Annotation score:

Annotation score:1 out of 5

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti6 – 10EPPHR → SPAP in AAA58415 (PubMed:1836978).Curated5
Sequence conflicti180 – 181PA → QL in AAA58415 (PubMed:1836978).Curated2

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_02093288S → F1 PublicationCorresponds to variant dbSNP:rs3731499Ensembl.1
Natural variantiVAR_023532182R → G1 PublicationCorresponds to variant dbSNP:rs6771386Ensembl.1
Natural variantiVAR_023533182R → W. Corresponds to variant dbSNP:rs6771386Ensembl.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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_000860144 – 183Missing in isoform 2. 2 PublicationsAdd BLAST40

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
M81933 mRNA Translation: AAA58415.1
AY137580 mRNA Translation: AAN11305.1
AF527417 Genomic DNA Translation: AAM77917.1
BC007401 mRNA Translation: AAH07401.1
BC018642 mRNA Translation: AAH18642.1
AF277722 mRNA Translation: AAG41884.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS2760.1 [P30304-1]
CCDS2761.1 [P30304-2]

Protein sequence database of the Protein Information Resource

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PIRi
A41648

NCBI Reference Sequences

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RefSeqi
NP_001780.2, NM_001789.2 [P30304-1]
NP_963861.1, NM_201567.1 [P30304-2]
XP_011532618.1, XM_011534316.1

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.437705

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000302506; ENSP00000303706; ENSG00000164045 [P30304-1]
ENST00000351231; ENSP00000343166; ENSG00000164045 [P30304-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
993

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:993

UCSC genome browser

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UCSCi
uc003csh.2 human [P30304-1]

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

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81933 mRNA Translation: AAA58415.1
AY137580 mRNA Translation: AAN11305.1
AF527417 Genomic DNA Translation: AAM77917.1
BC007401 mRNA Translation: AAH07401.1
BC018642 mRNA Translation: AAH18642.1
AF277722 mRNA Translation: AAG41884.1
CCDSiCCDS2760.1 [P30304-1]
CCDS2761.1 [P30304-2]
PIRiA41648
RefSeqiNP_001780.2, NM_001789.2 [P30304-1]
NP_963861.1, NM_201567.1 [P30304-2]
XP_011532618.1, XM_011534316.1
UniGeneiHs.437705

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C25X-ray2.30A337-496[»]
ProteinModelPortaliP30304
SMRiP30304
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107428, 80 interactors
DIPiDIP-166N
ELMiP30304
IntActiP30304, 44 interactors
MINTiP30304
STRINGi9606.ENSP00000303706

Chemistry databases

BindingDBiP30304
ChEMBLiCHEMBL3775

PTM databases

DEPODiP30304
iPTMnetiP30304
PhosphoSitePlusiP30304

Polymorphism and mutation databases

BioMutaiCDC25A
DMDMi50403734

Proteomic databases

EPDiP30304
MaxQBiP30304
PaxDbiP30304
PeptideAtlasiP30304
PRIDEiP30304
ProteomicsDBi54652
54653 [P30304-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
993
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302506; ENSP00000303706; ENSG00000164045 [P30304-1]
ENST00000351231; ENSP00000343166; ENSG00000164045 [P30304-2]
GeneIDi993
KEGGihsa:993
UCSCiuc003csh.2 human [P30304-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
993
DisGeNETi993
EuPathDBiHostDB:ENSG00000164045.11

GeneCards: human genes, protein and diseases

More...
GeneCardsi
CDC25A
HGNCiHGNC:1725 CDC25A
HPAiHPA005855
MIMi116947 gene
neXtProtiNX_P30304
OpenTargetsiENSG00000164045
PharmGKBiPA26259

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3772 Eukaryota
COG5105 LUCA
GeneTreeiENSGT00940000160737
HOGENOMiHOG000082672
HOVERGENiHBG052501
InParanoidiP30304
KOiK06645
OMAiPQSYRPM
OrthoDBiEOG091G0H0D
PhylomeDBiP30304
TreeFamiTF101056

Enzyme and pathway databases

BRENDAi3.1.3.48 2681
ReactomeiR-HSA-1362277 Transcription of E2F targets under negative control by DREAM complex
R-HSA-156711 Polo-like kinase mediated events
R-HSA-176187 Activation of ATR in response to replication stress
R-HSA-5689880 Ub-specific processing proteases
R-HSA-69202 Cyclin E associated events during G1/S transition
R-HSA-69273 Cyclin A/B1/B2 associated events during G2/M transition
R-HSA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry
R-HSA-8862803 Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models
SIGNORiP30304

Miscellaneous databases

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

More...
ChiTaRSi
CDC25A human
EvolutionaryTraceiP30304

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
CDC25A

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

More...
GenomeRNAii
993

Protein Ontology

More...
PROi
PR:P30304

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000164045 Expressed in 128 organ(s), highest expression level in secondary oocyte
CleanExiHS_CDC25A
ExpressionAtlasiP30304 baseline and differential
GenevisibleiP30304 HS

Family and domain databases

CDDicd01530 Cdc25, 1 hit
Gene3Di3.40.250.10, 1 hit
InterProiView protein in InterPro
IPR000751 MPI_Phosphatase
IPR001763 Rhodanese-like_dom
IPR036873 Rhodanese-like_dom_sf
PfamiView protein in Pfam
PF06617 M-inducer_phosp, 1 hit
PF00581 Rhodanese, 1 hit
PRINTSiPR00716 MPIPHPHTASE
SMARTiView protein in SMART
SM00450 RHOD, 1 hit
SUPFAMiSSF52821 SSF52821, 1 hit
PROSITEiView protein in PROSITE
PS50206 RHODANESE_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiMPIP1_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: P30304
Secondary accession number(s): Q8IZH5, Q96IL3, Q9H2F2
<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: April 1, 1993
Last sequence update: July 19, 2004
Last modified: December 5, 2018
This is version 184 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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