UniProtKB - P30305 (MPIP2_HUMAN)
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Protein
M-phase inducer phosphatase 2
Gene
CDC25B
Organism
Homo sapiens (Human)
Status
Functioni
Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Directly dephosphorylates CDK1 and stimulates its kinase activity. The three isoforms seem to have a different level of activity.1 Publication
Catalytic activityi
Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Enzyme regulationi
Stimulated by B-type cyclins.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Active sitei | 487 | 1 |
GO - Molecular functioni
- phosphoprotein phosphatase activity Source: Reactome
- protein kinase binding Source: UniProtKB
- protein tyrosine phosphatase activity Source: UniProtKB
GO - Biological processi
- cell division Source: UniProtKB-KW
- female meiosis I Source: Ensembl
- G2/M transition of mitotic cell cycle Source: UniProtKB
- mitotic cell cycle Source: UniProtKB
- oocyte maturation Source: Ensembl
- positive regulation of cell cycle G2/M phase transition Source: InterPro
- positive regulation of cell proliferation Source: ProtInc
- positive regulation of cytokinesis Source: UniProtKB
- positive regulation of mitotic cell cycle Source: UniProtKB
- positive regulation of protein kinase activity Source: Ensembl
- protein phosphorylation Source: UniProtKB
Keywordsi
| Molecular function | Hydrolase, Protein phosphatase |
| Biological process | Cell cycle, Cell division, Mitosis |
Enzyme and pathway databases
| BRENDAi | 3.1.3.48. 2681. |
| Reactomei | R-HSA-157881. Cyclin B2 mediated events. R-HSA-69273. Cyclin A/B1 associated events during G2/M transition. 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. |
| SIGNORi | P30305. |
Names & Taxonomyi
| Protein namesi | Recommended name: M-phase inducer phosphatase 2 (EC:3.1.3.48)Alternative name(s): Dual specificity phosphatase Cdc25B |
| Gene namesi | Name:CDC25B Synonyms:CDC25HU2 |
| Organismi | Homo sapiens (Human) |
| Taxonomic identifieri | 9606 [NCBI] |
| Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
| Proteomesi |
|
Organism-specific databases
| HGNCi | HGNC:1726. CDC25B. |
Subcellular locationi
- Cytoplasm › cytoskeleton › microtubule organizing center › centrosome 3 Publications
- Cytoplasm › cytoskeleton › spindle pole 1 Publication
GO - Cellular componenti
- centrosome Source: UniProtKB
- cytosol Source: Reactome
- nucleoplasm Source: Reactome
- spindle pole Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, CytoskeletonPathology & Biotechi
Organism-specific databases
| DisGeNETi | 994. |
| OpenTargetsi | ENSG00000101224. |
| PharmGKBi | PA26260. |
Chemistry databases
| ChEMBLi | CHEMBL4804. |
| DrugBanki | DB03661. Cysteinesulfonic Acid. |
Polymorphism and mutation databases
| DMDMi | 21264471. |
PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| ChainiPRO_0000198644 | 1 – 580 | M-phase inducer phosphatase 2Add BLAST | 580 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Modified residuei | 42 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 169 | Phosphoserine; by MELK1 Publication | 1 | |
| Modified residuei | 249 | PhosphoserineCombined sources | 1 | |
| Modified residuei | 323 | Phosphoserine; by MELK and MAPK14Combined sources3 Publications | 1 | |
| Modified residuei | 353 | Phosphoserine; by AURKACombined sources1 Publication | 1 | |
| Modified residuei | 375 | Phosphoserine; by BRSK1 and MAPK14Combined sources2 Publications | 1 | |
| Modified residuei | 470 | PhosphoserineCombined sources | 1 | |
| Modified residuei | 563 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Phosphorylated by BRSK1 in vitro. Phosphorylated by CHEK1, which inhibits the activity of this protein. Phosphorylation at Ser-353 by AURKA might locally participate in the control of the onset of mitosis. Phosphorylation by MELK at Ser-169 promotes localization to the centrosome and the spindle poles during mitosis. Phosphorylation at Ser-323 and Ser-375 by MAPK14 is required for binding to 14-3-3 proteins.8 Publications
Keywords - PTMi
PhosphoproteinProteomic databases
| EPDi | P30305. |
| MaxQBi | P30305. |
| PaxDbi | P30305. |
| PeptideAtlasi | P30305. |
| PRIDEi | P30305. |
PTM databases
| DEPODi | P30305. |
| iPTMneti | P30305. |
| PhosphoSitePlusi | P30305. |
Expressioni
Gene expression databases
| Bgeei | ENSG00000101224. |
| CleanExi | HS_CDC25B. |
| ExpressionAtlasi | P30305. baseline and differential. |
| Genevisiblei | P30305. HS. |
Organism-specific databases
| HPAi | HPA038892. HPA038893. |
Interactioni
Subunit structurei
Interacts with MAPK14 and 14-3-3 proteins.1 Publication
Binary interactionsi
GO - Molecular functioni
- protein kinase binding Source: UniProtKB
Protein-protein interaction databases
| BioGridi | 107429. 34 interactors. |
| DIPi | DIP-323N. |
| IntActi | P30305. 16 interactors. |
| MINTi | MINT-124404. |
| STRINGi | 9606.ENSP00000245960. |
Chemistry databases
| BindingDBi | P30305. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Beta strandi | 396 – 399 | Combined sources | 4 | |
| Helixi | 417 – 424 | Combined sources | 8 | |
| Turni | 425 – 431 | Combined sources | 7 | |
| Beta strandi | 432 – 439 | Combined sources | 8 | |
| Helixi | 443 – 447 | Combined sources | 5 | |
| Helixi | 460 – 468 | Combined sources | 9 | |
| Turni | 469 – 471 | Combined sources | 3 | |
| Beta strandi | 479 – 486 | Combined sources | 8 | |
| Beta strandi | 488 – 492 | Combined sources | 5 | |
| Helixi | 493 – 508 | Combined sources | 16 | |
| Beta strandi | 519 – 522 | Combined sources | 4 | |
| Helixi | 525 – 532 | Combined sources | 8 | |
| Helixi | 534 – 536 | Combined sources | 3 | |
| Beta strandi | 537 – 540 | Combined sources | 4 | |
| Helixi | 548 – 550 | Combined sources | 3 | |
| Helixi | 551 – 558 | Combined sources | 8 |
3D structure databases
| Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1CWR | X-ray | 2.10 | A | 370-580 | [»] | |
| 1CWS | X-ray | 2.00 | A | 370-580 | [»] | |
| 1CWT | X-ray | 2.30 | A | 388-565 | [»] | |
| 1QB0 | X-ray | 1.91 | A | 370-580 | [»] | |
| 1YM9 | X-ray | 2.00 | A | 391-564 | [»] | |
| 1YMD | X-ray | 1.70 | A | 391-564 | [»] | |
| 1YMK | X-ray | 1.70 | A | 391-564 | [»] | |
| 1YML | X-ray | 1.70 | A | 391-564 | [»] | |
| 1YS0 | X-ray | 2.00 | A | 391-564 | [»] | |
| 2A2K | X-ray | 1.52 | A | 391-564 | [»] | |
| 2IFD | X-ray | 2.00 | A | 391-564 | [»] | |
| 2IFV | X-ray | 1.60 | A | 391-564 | [»] | |
| 2UZQ | X-ray | 2.38 | A/B/C/D/E/F | 391-580 | [»] | |
| 3FQT | X-ray | 1.80 | C | 38-46 | [»] | |
| 3FQU | X-ray | 1.80 | C | 38-46 | [»] | |
| 4WH7 | X-ray | 1.62 | A | 386-565 | [»] | |
| 4WH9 | X-ray | 1.50 | A | 386-565 | [»] | |
| ProteinModelPortali | P30305. | |||||
| SMRi | P30305. | |||||
| ModBasei | Search... | |||||
| MobiDBi | Search... | |||||
Miscellaneous databases
| EvolutionaryTracei | P30305. |
Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Domaini | 431 – 538 | RhodanesePROSITE-ProRule annotationAdd BLAST | 108 |
Sequence similaritiesi
Belongs to the MPI phosphatase family.Curated
Phylogenomic databases
| eggNOGi | KOG3772. Eukaryota. COG5105. LUCA. |
| GeneTreei | ENSGT00390000018747. |
| HOVERGENi | HBG052501. |
| InParanoidi | P30305. |
| KOi | K05866. |
| OMAi | THALAEW. |
| OrthoDBi | EOG091G0H0D. |
| PhylomeDBi | P30305. |
| TreeFami | TF101056. |
Family and domain databases
| Gene3Di | 3.40.250.10. 1 hit. |
| InterProi | View protein in InterPro IPR000751. MPI_Phosphatase. IPR001763. Rhodanese-like_dom. |
| Pfami | View protein in Pfam PF06617. M-inducer_phosp. 1 hit. PF00581. Rhodanese. 1 hit. |
| PRINTSi | PR00716. MPIPHPHTASE. |
| SMARTi | View protein in SMART SM00450. RHOD. 1 hit. |
| SUPFAMi | SSF52821. SSF52821. 1 hit. |
| PROSITEi | View protein in PROSITE PS50206. RHODANESE_3. 1 hit. |
Sequences (4)i
Sequence statusi: Complete.
This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 3 (identifier: P30305-1) [UniParc]FASTAAdd to basket
Also known as: CDC25B3
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.
10 20 30 40 50
MEVPQPEPAP GSALSPAGVC GGAQRPGHLP GLLLGSHGLL GSPVRAAASS
60 70 80 90 100
PVTTLTQTMH DLAGLGSETP KSQVGTLLFR SRSRLTHLSL SRRASESSLS
110 120 130 140 150
SESSESSDAG LCMDSPSPMD PHMAEQTFEQ AIQAASRIIR NEQFAIRRFQ
160 170 180 190 200
SMPVRLLGHS PVLRNITNSQ APDGRRKSEA GSGAASSSGE DKENDGFVFK
210 220 230 240 250
MPWKPTHPSS THALAEWASR REAFAQRPSS APDLMCLSPD RKMEVEELSP
260 270 280 290 300
LALGRFSLTP AEGDTEEDDG FVDILESDLK DDDAVPPGME SLISAPLVKT
310 320 330 340 350
LEKEEEKDLV MYSKCQRLFR SPSMPCSVIR PILKRLERPQ DRDTPVQNKR
360 370 380 390 400
RRSVTPPEEQ QEAEEPKARV LRSKSLCHDE IENLLDSDHR ELIGDYSKAF
410 420 430 440 450
LLQTVDGKHQ DLKYISPETM VALLTGKFSN IVDKFVIVDC RYPYEYEGGH
460 470 480 490 500
IKTAVNLPLE RDAESFLLKS PIAPCSLDKR VILIFHCEFS SERGPRMCRF
510 520 530 540 550
IRERDRAVND YPSLYYPEMY ILKGGYKEFF PQHPNFCEPQ DYRPMNHEAF
560 570 580
KDELKTFRLK TRSWAGERSR RELCSRLQDQ
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Sequence conflicti | 575 | S → D in AAB21139 (PubMed:1662986).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_020933 | 548 | E → K1 PublicationCorresponds to variant dbSNP:rs11570019Ensembl. | 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Alternative sequenceiVSP_000861 | 68 – 81 | Missing in isoform 1 and isoform 4. 2 PublicationsAdd BLAST | 14 | |
| Alternative sequenceiVSP_000862 | 154 – 194 | Missing in isoform 2. 1 PublicationAdd BLAST | 41 | |
| Alternative sequenceiVSP_012587 | 194 | N → NVRFWKAGVGALREEEGACW GGSLACEDPPLPSWLQ in isoform 4. Curated | 1 |
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M81934 mRNA. Translation: AAA58416.1. S78187 mRNA. Translation: AAB21139.1. X96436 Genomic DNA. Translation: CAA65303.1. Z68092 mRNA. Translation: CAA92108.1. AY494082 Genomic DNA. Translation: AAR26469.1. AL109804 Genomic DNA. Translation: CAC17548.1. AL109804 Genomic DNA. Translation: CAC17549.1. AL109804 Genomic DNA. Translation: CAI18847.1. CH471133 Genomic DNA. Translation: EAX10491.1. CH471133 Genomic DNA. Translation: EAX10492.1. CH471133 Genomic DNA. Translation: EAX10493.1. CH471133 Genomic DNA. Translation: EAX10494.1. CH471133 Genomic DNA. Translation: EAX10496.1. CH471133 Genomic DNA. Translation: EAX10497.1. CH471133 Genomic DNA. Translation: EAX10498.1. CH471133 Genomic DNA. Translation: EAX10499.1. BC006395 mRNA. Translation: AAH06395.1. BC009953 mRNA. Translation: AAH09953.1. BC051711 mRNA. Translation: AAH51711.1. AF036233 Genomic DNA. Translation: AAB94622.1. AF036233 Genomic DNA. Translation: AAB94624.1. |
| CCDSi | CCDS13065.1. [P30305-2] CCDS13066.1. [P30305-3] CCDS13067.1. [P30305-1] |
| PIRi | B41648. |
| RefSeqi | NP_001274448.1. NM_001287519.1. NP_001274453.1. NM_001287524.1. NP_004349.1. NM_004358.4. [P30305-2] NP_068658.1. NM_021872.3. [P30305-3] NP_068659.1. NM_021873.3. [P30305-1] |
| UniGenei | Hs.153752. |
Genome annotation databases
| Ensembli | ENST00000245960; ENSP00000245960; ENSG00000101224. [P30305-1] ENST00000340833; ENSP00000339170; ENSG00000101224. [P30305-3] ENST00000439880; ENSP00000405972; ENSG00000101224. [P30305-2] |
| GeneIDi | 994. |
| KEGGi | hsa:994. |
| UCSCi | uc002wjn.5. human. [P30305-1] |
Keywords - Coding sequence diversityi
Alternative splicing, PolymorphismSimilar proteinsi
Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:| 100% | UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry. |
| 90% | UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence). |
| 50% | UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster. |
Entry informationi
| Entry namei | MPIP2_HUMAN | |
| Accessioni | P30305Primary (citable) accession number: P30305 Secondary accession number(s): D3DVY1 Q9BRA6 | |
| Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1993 |
| Last sequence update: | May 27, 2002 | |
| Last modified: | June 7, 2017 | |
| This is version 183 of the entry and version 2 of the sequence. See complete history. | ||
| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any 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. | |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 20
Human chromosome 20: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
