Your IP: 38.107.179.212 United States Near: United States

Lookup IP Information

1 2 3 4 5 6 7 8 Next

Below is the list of all allocated IP address in 7.23.0.0 - 7.23.255.255 network range, sorted by latency.

edit Cell division cycle 25 homolog B (S. pombe) PDB rendering based on 1cwr. Available structures PDB 1cwr, 1cws, 1cwt, 1qb0, 1ym9, 1ymd, 1ymk, 1yml, 1ys0, 2a2k, 2ifd, 2ifv Identifiers Symbols CDC25B; External IDs OMIM: 116949 MGI: 99701 HomoloGene: 41451 GeneCards: CDC25B Gene Gene Ontology Molecular function • protein tyrosine phosphatase activity • hydrolase activity Cellular component • intracellular Biological process • regulation of progression through cell cycle • M phase of mitotic cell cycle • protein amino acid dephosphorylation • mitosis • positive regulation of cell proliferation • cell division Sources: Amigo / EGO RNA expression pattern More reference expression data Orthologs Species Human Mouse Entrez 994 12531 Ensembl ENSG00000101224 ENSMUSG00000027330 UniProt P30305 Q3U535 RefSeq (mRNA) NM_004358 XM_988699 RefSeq (protein) NP_004349 XP_993793 Location (UCSC) Chr 20: 3.72 - 3.73 Mb Chr 2: 130.88 - 130.89 Mb PubMed search [1] [2] 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 (Feb 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)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=994.  ^ 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 (Jan. 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 (Sep. 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 (Oct. 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 (Dec. 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. PMID 11689696.  ^ a b c d Mils, V; Baldin V, Goubin F, Pinta I, Papin C, Waye M, Eychene A, Ducommun B (Mar. 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.  ^ a b Conklin, D S; Galaktionov K, Beach D (Aug. 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. PMID 7644510.  Further reading Draetta G, Eckstein J (1997). "Cdc25 protein phosphatases in cell proliferation.". Biochim. Biophys. Acta 1332 (2): M53–63. PMID 9141461.  Nilsson I, Hoffmann I (2000). "Cell cycle regulation by the Cdc25 phosphatase family.". Progress in cell cycle research 4: 107–14. 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. 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. 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. 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.  v • d • e 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   This article on a gene on chromosome 20 is a stub. You can help Wikipedia by expanding it. v • d • e v • d • e 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, PTPRZ) Non receptor type PTPs (PTPN1, PTPN2, PTPN3, PTPN4, PTPN5, PTPN6, PTPN7, PTPN9, PTPN11, PTPN12, PTPN13, PTPN14, PTPN18, PTPN20, PTPN21, PTPN22, PTPN23 Class I 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 CDC25A, CDC25B, CDC25C Class IV EYA1 (Eya1, Eya2, Eya3, Eya4)