CDC25B

Cell division cycle 25B

PDB rendering based on 1cwr.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1CWR, 1CWS, 1CWT, 1QB0, 1YM9, 1YMD, 1YMK, 1YML, 1YS0, 2A2K, 2IFD, 2IFV, 2UZQ, 3FQT, 3FQU, 4WH7, 4WH9

Identifiers

Symbol

CDC25B

External IDs

OMIM: 116949 MGI: 99701 HomoloGene: 41451 ChEMBL: 4804 GeneCards: CDC25B Gene

EC number

3.1.3.48

Gene ontology
Molecular function	• protein tyrosine phosphatase activity • protein binding • protein kinase binding
Cellular component	• spindle pole • nucleoplasm • cytoplasm • centrosome • cytosol
Biological process	• G2/M transition of mitotic cell cycle • mitotic cell cycle • oocyte maturation • protein phosphorylation • mitotic nuclear division • female meiosis I • positive regulation of cell proliferation • positive regulation of cytokinesis • peptidyl-tyrosine dephosphorylation • positive regulation of protein kinase activity • positive regulation of mitotic cell cycle • cell division
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

994

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 20:
3.79 – 3.81 Mb

Chr 2:
131.19 – 131.2 Mb

PubMed search

M-phase inducer phosphatase 2 is an enzyme that in humans is encoded by the CDC25B gene.^[1]

CDC25B is a member of the CDC25 family of phosphatases. CDC25B activates the cyclin dependent kinase CDC2 by removing two phosphate groups and it is required for entry into mitosis. CDC25B shuttles between the nucleus and the cytoplasm due to nuclear localization and nuclear export signals. The protein is nuclear in the M and G1 phases of the cell cycle and moves to the cytoplasm during S and G2. CDC25B has oncogenic properties, although its role in tumor formation has not been determined. Multiple transcript variants for this gene exist.^[2]

Interactions

CDC25B has been shown to interact with MAPK14,^[3] Casein kinase 2, alpha 1,^[4] CHEK1,^[5] MELK,^[6] Estrogen receptor alpha,^[7] YWHAB,^[8]^[9] YWHAZ,^[8] YWHAH^[8] and YWHAE.^[8]^[9]

References

↑ Galaktionov K, Beach D (February 1992). "Specific activation of cdc25 tyrosine phosphatases by B-type cyclins: evidence for multiple roles of mitotic cyclins". Cell 67 (6): 1181–94. doi:10.1016/0092-8674(91)90294-9. PMID 1836978.
↑ "Entrez Gene: CDC25B cell division cycle 25 homolog B (S. pombe)".
↑ Bulavin, D V; Higashimoto Y; Popoff I J; Gaarde W A; Basrur V; Potapova O; Appella E; Fornace A J (May 2001). "Initiation of a G2/M checkpoint after ultraviolet radiation requires p38 kinase". Nature (England) 411 (6833): 102–7. doi:10.1038/35075107. ISSN 0028-0836. PMID 11333986.
↑ Theis-Febvre, Nathalie; Filhol Odile; Froment Carine; Cazales Martine; Cochet Claude; Monsarrat Bernard; Ducommun Bernard; Baldin Véronique (January 2003). "Protein kinase CK2 regulates CDC25B phosphatase activity". Oncogene (England) 22 (2): 220–32. doi:10.1038/sj.onc.1206107. ISSN 0950-9232. PMID 12527891.
↑ Sanchez, Y; Wong C; Thoma R S; Richman R; Wu Z; Piwnica-Worms H; Elledge S J (September 1997). "Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to Cdk regulation through Cdc25". Science (UNITED STATES) 277 (5331): 1497–501. doi:10.1126/science.277.5331.1497. ISSN 0036-8075. PMID 9278511.
↑ Davezac, Noélie; Baldin Véronique; Blot Joëlle; Ducommun Bernard; Tassan Jean-Pierre (October 2002). "Human pEg3 kinase associates with and phosphorylates CDC25B phosphatase: a potential role for pEg3 in cell cycle regulation". Oncogene (England) 21 (50): 7630–41. doi:10.1038/sj.onc.1205870. ISSN 0950-9232. PMID 12400006.
↑ Ma, Z Q; Liu Z; Ngan E S; Tsai S Y (December 2001). "Cdc25B Functions as a Novel Coactivator for the Steroid Receptors". Mol. Cell. Biol. (United States) 21 (23): 8056–67. doi:10.1128/MCB.21.23.8056-8067.2001. ISSN 0270-7306. PMC 99972. PMID 11689696.
1 2 3 4 Mils, V; Baldin V; Goubin F; Pinta I; Papin C; Waye M; Eychene A; Ducommun B (March 2000). "Specific interaction between 14-3-3 isoforms and the human CDC25B phosphatase". Oncogene (ENGLAND) 19 (10): 1257–65. doi:10.1038/sj.onc.1203419. ISSN 0950-9232. PMID 10713667.
1 2 Conklin, D S; Galaktionov K; Beach D (August 1995). "14-3-3 proteins associate with cdc25 phosphatases". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 92 (17): 7892–6. doi:10.1073/pnas.92.17.7892. ISSN 0027-8424. PMC 41252. PMID 7644510.

Draetta G, Eckstein J (1997). "Cdc25 protein phosphatases in cell proliferation". Biochim. Biophys. Acta 1332 (2): M53–63. doi:10.1016/S0304-419X(96)00049-2. PMID 9141461.
Nilsson I, Hoffmann I (2000). "Cell cycle regulation by the Cdc25 phosphatase family". Progress in cell cycle research 4: 107–14. doi:10.1007/978-1-4615-4253-7_10. PMID 10740819.
Nagata A, Igarashi M, Jinno S; et al. (1992). "An additional homolog of the fission yeast cdc25+ gene occurs in humans and is highly expressed in some cancer cells". New Biol. 3 (10): 959–68. PMID 1662986.
Conklin DS, Galaktionov K, Beach D (1995). "14-3-3 proteins associate with cdc25 phosphatases". Proc. Natl. Acad. Sci. U.S.A. 92 (17): 7892–6. doi:10.1073/pnas.92.17.7892. PMC 41252. PMID 7644510.
Galaktionov K, Lee AK, Eckstein J; et al. (1995). "CDC25 phosphatases as potential human oncogenes". Science 269 (5230): 1575–7. doi:10.1126/science.7667636. PMID 7667636.
Demetrick DJ, Beach DH (1994). "Chromosome mapping of human CDC25A and CDC25B phosphatases". Genomics 18 (1): 144–7. doi:10.1006/geno.1993.1440. PMID 8276402.
Honda R, Ohba Y, Nagata A; et al. (1993). "Dephosphorylation of human p34cdc2 kinase on both Thr-14 and Tyr-15 by human cdc25B phosphatase". FEBS Lett. 318 (3): 331–4. doi:10.1016/0014-5793(93)80540-B. PMID 8440392.
Lane SA, Baker E, Sutherland GR; et al. (1993). "The human cell cycle gene CDC25B is located at 20p13". Genomics 15 (3): 693–4. doi:10.1006/geno.1993.1129. PMID 8468065.
Baldin V, Cans C, Superti-Furga G, Ducommun B (1997). "Alternative splicing of the human CDC25B tyrosine phosphatase. Possible implications for growth control?". Oncogene 14 (20): 2485–95. doi:10.1038/sj.onc.1201063. PMID 9188863.
Booher RN, Holman PS, Fattaey A (1997). "Human Myt1 is a cell cycle-regulated kinase that inhibits Cdc2 but not Cdk2 activity". J. Biol. Chem. 272 (35): 22300–6. doi:10.1074/jbc.272.35.22300. PMID 9268380.
Sanchez Y, Wong C, Thoma RS; et al. (1997). "Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to Cdk regulation through Cdc25". Science 277 (5331): 1497–501. doi:10.1126/science.277.5331.1497. PMID 9278511.
Jin P, Hardy S, Morgan DO (1998). "Nuclear Localization of Cyclin B1 Controls Mitotic Entry After DNA Damage". J. Cell Biol. 141 (4): 875–85. doi:10.1083/jcb.141.4.875. PMC 2132764. PMID 9585407.
Hofmann K, Bucher P, Kajava AV (1998). "A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain". J. Mol. Biol. 282 (1): 195–208. doi:10.1006/jmbi.1998.1998. PMID 9733650.
Forrest AR, McCormack AK, DeSouza CP; et al. (1999). "Multiple splicing variants of cdc25B regulate G2/M progression". Biochem. Biophys. Res. Commun. 260 (2): 510–5. doi:10.1006/bbrc.1999.0870. PMID 10403798.
Karlsson C, Katich S, Hagting A; et al. (1999). "Cdc25b and Cdc25c Differ Markedly in Their Properties as Initiators of Mitosis". J. Cell Biol. 146 (3): 573–84. doi:10.1083/jcb.146.3.573. PMC 2150562. PMID 10444066.
Reynolds RA, Yem AW, Wolfe CL; et al. (1999). "Crystal structure of the catalytic subunit of Cdc25B required for G2/M phase transition of the cell cycle". J. Mol. Biol. 293 (3): 559–68. doi:10.1006/jmbi.1999.3168. PMID 10543950.
Mils V, Baldin V, Goubin F; et al. (2000). "Specific interaction between 14-3-3 isoforms and the human CDC25B phosphatase". Oncogene 19 (10): 1257–65. doi:10.1038/sj.onc.1203419. PMID 10713667.

PDB gallery

1cwr: HUMAN CDC25B CATALYTIC DOMAIN WITHOUT ION IN CATALYTIC SITE

1cws: HUMAN CDC25B CATALYTIC DOMAIN WITH TUNGSTATE

1cwt: HUMAN CDC25B CATALYTIC DOMAIN WITH METHYL MERCURY

1qb0: HUMAN CDC25B CATALYTIC DOMAIN

1ym9: Crystal structure of the CDC25B phosphatase catalytic domain with the active site cysteine in the sulfinic form

1ymd: Crystal Structure of the CDC25B phosphatase catalytic domain with the active site cysteine in the sulfonic form

1ymk: Crystal Structure of the CDC25B phosphatase catalytic domain in the apo form

1yml: Crystal Structure of the CDC25B phosphatase catalytic domain with the active site cysteine in the sulfenic form

1ys0: Crystal Structure of the CDC25B phosphatase catalytic domain with the active site cysteine in the disulfide form

2a2k: Crystal Structure of an active site mutant, C473S, of Cdc25B Phosphatase Catalytic Domain

2ifd: Crystal structure of a remote binding site mutant, R492L, of CDC25B Phosphatase catalytic domain

2ifv: Crystal structure of an active site mutant, C473D, of CDC25B phosphatase catalytic domain

Esterase: protein tyrosine phosphatases (EC 3.1.3.48)

Class I

Classical PTPs

Receptor type PTPs	PTPRA PTPRB PTPRC PTPRD PTPRE PTPRF PTPRG PTPRH PTPRJ PTPRK PTPRM PTPRN PTPRN2 PTPRO PTPRQ PTPRR PTPRS PTPRT PTPRU PTPRZ1 PTPRZ2

Non receptor type PTPs	PTPN1 PTPN2 PTPN3 PTPN4 PTPN5 PTPN6 PTPN7 PTPN9 PTPN11 PTPN12 PTPN13 PTPN14 PTPN18 PTPN20 PTPN21 PTPN22 PTPN23

VH1-like or
dual specific
phosphatases
(DSPs)

MAPK phosphatases (MKPs)	DUSP1 DUSP2 DUSP4 DUSP5 DUSP6 DUSP7 DUSP8 DUSP9 DUSP10 DUSP16 MK-STYX

Slingshots	SSH1 SSH2 SSH3

PRLs	PTP4A1 PTP4A2 PTP4A3

CDC14s	CDC14A CDC14B CDKN3 PTP9Q22

Atypical DSPs	DUSP3 DUSP11 DUSP12 DUSP13A DUSP13B DUSP14 DUSP15 DUSP18 DUSP19 DUSP21 DUSP22 DUSP23 DUSP24 DUSP25 DUSP26 DUSP27 EMP2A RNGTT STYX

Phosphatase and tensin homologs (PTENs)	PTEN TPIP TPTE TNS TENC1

Myotubularins	MTM1 MTMR2 MTMR3 MTMR4 MTMR5 MTMR6 MTMR7 MTMR8 MTMR9 MTMR10 MTMR11 MTMR12 MTMR13 MTMR14 MTMR15

Class II

ACP1

Class III

Cdc25
- CDC25A
- CDC25B
- CDC25C

Class IV

EYA1
EYA2
EYA3
EYA4

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CDC25B

Interactions

References

Further reading