Human protein: IPI00291990 * 64987 Da * CDC25B Isoform 3 of M-phase inducer phosphatase 2 - Liebel-Lab @ KIT
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>CDC25B Isoform 3 of M-phase inducer phosphatase 2 - Length: 580 AS 
MEVPQPEPAPGSALSPAGVCGGAQRPGHLPGLLLGSHGLLGSPVRAAASSPVTTLTQTMHDLAGLGSETPKSQVGTLLFR
SRSRLTHLSLSRRASESSLSSESSESSDAGLCMDSPSPMDPHMAEQTFEQAIQAASRIIRNEQFAIRRFQSMPVRLLGHS
PVLRNITNSQAPDGRRKSEAGSGAASSSGEDKENDGFVFKMPWKPTHPSSTHALAEWASRREAFAQRPSSAPDLMCLSPD
RKMEVEELSPLALGRFSLTPAEGDTEEDDGFVDILESDLKDDDAVPPGMESLISAPLVKTLEKEEEKDLVMYSKCQRLFR
SPSMPCSVIRPILKRLERPQDRDTPVQNKRRRSVTPPEEQQEAEEPKARVLRSKSLCHDEIENLLDSDHRELIGDYSKAF
LLQTVDGKHQDLKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIAPCSLDKR
VILIFHCEFSSERGPRMCRFIRERDRAVNDYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPMNHEAFKDELKTFRLK
TRSWAGERSRRELCSRLQDQ
Linkouts to other data resources: BioCompare * Entrez * PolyMeta * GeneCard * imaGenes * GenomeBrowser * Google Scholar * Mitocheck
AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page
Diseaselink to OMIM


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page
ACTIVATE: SMART analysis
NameBeginEndE-value
low complexity2643-
low complexity77107-
Pfam:M-inducer_phosp1133841.80e-166
RHOD4215352.18e-27

These features and domains are not shown in the diagram, either because their scores are less significant than the required threshold, or because they overlap with some other source of annotation:

NameBeginEndE-valueReason
low complexity178190-overlap
low complexity356366-overlap
Pfam:Rhodanese4245322.50e-36overlap


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page

AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page

AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page

AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page
General information
Entry name MPIP2_HUMAN
Accession number P30305, O43551, Q13971, Q5JX77, Q6RSS1, Q9BRA6
Integrated 01-APR-1993, UniProtKB/Swiss-Prot.
Sequence update 27-MAY-2002, sequence version 2
Annotation update 25-NOV-2008, entry version 101
UniSave P30305, O43551, Q13971, Q5JX77, Q6RSS1, Q9BRA6
UniRef100 UniRef100_P30305, UniRef100_P30305-4, UniRef100_P30305-3, UniRef100_P30305-2
UniParc UPI000002AE3B, UPI000002AE3C, UPI000012F474, UPI000013CBC5
Description and origin of the Protein
Description Recommended
Full=M-phase inducer phosphatase 2;
EC=3.1.3.48;
Synonym
Full=Dual specificity phosphatase Cdc25B;
Gene name(s) CDC25B
Synonym(s) CDC25HU2
Organism source Homo sapiens (Human).
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
NCBI TaxID 9606
References
[1] Galaktionov,K.I., Beach,D.,
Specific activation of cdc25 tyrosine phosphatases by B-type cyclins: evidence for multiple roles of mitotic cyclins.
(1991) Cell 67:1181-1194
Position NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Medline 92103683
DOI 10.1016/0092-8674(91)90294-9;
PubMed
1836978 Subscription requiredClick to get it from ScienceDirect CiteXplore
[2] Nagata,A., Igarashi,M., Jinno,S., Suto,K., Okayama,H.,
An additional homolog of the fission yeast cdc25+ gene occurs in humans and is highly expressed in some cancer cells.
(1991) New Biol. 3:959-968
Position NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Medline 92118716
PubMed
1662986 CiteXplore
[3] Baldin,V., Cans,C., Superti-Furga,G., Docommun,B.,
Alternative splicing of the human CDC25B tyrosine phosphatase. Possible implications for growth control?
(1997) Oncogene 14:2485-2495
Position NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3).
Medline 97332629
DOI 10.1038/sj.onc.1201063;
PubMed
9188863 Subscription requiredClick to get it from nature.com Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[4] Livingston,R.J., Rieder,M.J., Chung,M.-W., Ritchie,T.K., Olson,A.N., Nguyen,C.P., Nguyen,D.A., Poel,C.L., Robertson,P.D., Schackwitz,W.S., Sherwood,J.K., Sherwood,A.M., Leithauser,B.J., Nickerson,D.A.,
NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).
Submitted DEC-2003 to the EMBL GenBank DDBJ databases
Position NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-548.
[5] Deloukas,P., Matthews,L.H., Ashurst,J.L., Burton,J., Gilbert,J.G.R., Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L., Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M., Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J., Buck,D., Burrill,W.D., Butler,A.P., Carder,C., Carter,N.P., Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y., Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.E., Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.D., Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L., Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N.D., Gwilliam,R., Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L., Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K., Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A., Knights,A., Laird,G.K., Lawlor,S., Lehvaeslaiho,M.H., Leversha,M.A., Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L., McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S.A., Mistry,D., Moore,M.J.F., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A., Patel,R., Pearce,T.A.V., Peck,A.I., Phillimore,B.J.C.T., Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T., Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D., Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,R.M., Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L., Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L., Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S., Rogers,J.,
The DNA sequence and comparative analysis of human chromosome 20.
(2001) Nature 414:865-871
Position NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Medline 21638749
DOI 10.1038/414865a;
PubMed
11780052 Subscription requiredClick to get it from nature.com Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[6]
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
(2004) Genome Res. 14:2121-2127
Position NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Comments TISSUE=Brain;
DOI 10.1101/gr.2596504;
PubMed
15489334 Free after 6 monthsClick to get it from www.genome.org Free after 6 monthsClick to get it from www.genome.org FreeClick to get it from www.genome.org Subscription requiredClick to get it from DOI Subscription requiredClick to get it from PaperBase@EBI FreeClick to get it from PubMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from UK_PubMedCentral FreeClick to get it from UK_PubMedCentral CiteXplore
[7] McCormack,A.K., DeSouza,C.C.P.C., Tonks,I.D., Clark,J.M., Forrest,A.R.R., Hayward,N.K., Ellem,K.A.O., Gabrielli,B.G.,
Alternative splicing of cdc25B.
Submitted NOV-1997 to the EMBL GenBank DDBJ databases
Position NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-352 (ISOFORMS 2 AND 3).
[8] Kraemer,A., Mailand,N., Lukas,C., Syljuaesen,R.G., Wilkinson,C.J., Nigg,E.A., Bartek,J., Lukas,J.,
Centrosome-associated Chk1 prevents premature activation of cyclin-B- Cdk1 kinase.
(2004) Nat. Cell Biol. 6:884-891
Position SUBCELLULAR LOCATION, AND PHOSPHORYLATION BY CHEK1.
DOI 10.1038/ncb1165;
PubMed
15311285 Subscription requiredClick to get it from nature.com Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[9] Reynolds,R.A., Yem,A.W., Wolfe,C.L., Deibel,M.R. Jr., Chidester,C.G., Watenpaugh,K.D.,
Crystal structure of the catalytic subunit of Cdc25B required for G2/M phase transition of the cell cycle.
(1999) J. Mol. Biol. 293:559-568
Position X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 370-580.
Medline 20013068
DOI 10.1006/jmbi.1999.3168;
PubMed
10543950 Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from ScienceDirect CiteXplore
Comments
FUNCTION Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Directly dephosphorylates CDC2 and stimulates its kinase activity. The three isoforms seem to have a different level of activity.
CATALYTIC ACTIVITY Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.
ENZYME REGULATION Stimulated by B-type cyclins.
INTERACTION
Q15323:KRT31 NbExp=1 IntAct=EBI-1051746, EBI-948001
P78386:KRT85 NbExp=1 IntAct=EBI-1051746, EBI-1049371
Q99623:PHB2 NbExp=1 IntAct=EBI-1051746, EBI-358348
SUBCELLULAR LOCATION Centrosome.
ALTERNATIVE PRODUCTS Event=Alternative splicing; Named isoforms=4;
Name=3; Synonyms=CDC25B3;
IsoId=P30305-1; Sequence=Displayed;
Name=1; Synonyms=CDC25B1;
IsoId=P30305-2; Sequence=VSP_000861;
Name=2; Synonyms=CDC25B2;
IsoId=P30305-3; Sequence=VSP_000862;
Name=4;
IsoId=P30305-4; Sequence=VSP_000861, VSP_012587;
Note=No experimental confirmation available;
PTM Phosphorylated by BRSK1 in vitro. Phosphorylated by CHEK1, which inhibits the activity of this protein.
SIMILARITY Belongs to the MPI phosphatase family.
SIMILARITY Contains 1 rhodanese domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms Distributed under the Creative Commons Attribution-NoDerivs License
Database cross-references
EMBL
M81934; AAA58416.1; -; mRNA.
S78187; AAB21139.1; -; mRNA.
X96436; CAA65303.1; -; Genomic_DNA.
Z68092; CAA92108.1; -; mRNA.
AY494082; AAR26469.1; -; Genomic_DNA.
AL109804; CAC17548.1; -; Genomic_DNA.
AL109804; CAC17549.1; -; Genomic_DNA.
AL109804; CAI18847.1; -; Genomic_DNA.
BC006395; AAH06395.1; -; mRNA.
BC009953; AAH09953.1; -; mRNA.
BC051711; AAH51711.1; -; mRNA.
AF036233; AAB94622.1; -; Genomic_DNA.
AF036233; AAB94624.1; -; Genomic_DNA.
PIR
B41648; B41648.
RefSeq
NP_068659.1; -.
UniGene
Hs.153752; -.
PDB
1CWR; X-ray; 2.10 A; A=370-580.
1CWS; X-ray; 2.00 A; A=370-580.
1CWT; X-ray; 2.30 A; A=388-565.
1QB0; X-ray; 1.91 A; A=370-580.
1YM9; X-ray; 2.00 A; A=391-564.
1YMD; X-ray; 1.70 A; A=391-564.
1YMK; X-ray; 1.70 A; A=391-564.
1YML; X-ray; 1.70 A; A=391-564.
1YS0; X-ray; 2.00 A; A=391-564.
2A2K; X-ray; 1.52 A; A=391-564.
2IFD; X-ray; 2.00 A; A=391-564.
2IFV; X-ray; 1.60 A; A=391-564.
2UZQ; X-ray; 2.38 A; A/B/C/D/E/F=391-580.
PDBsum
1CWR; -.
1CWS; -.
1CWT; -.
1QB0; -.
1YM9; -.
1YMD; -.
1YMK; -.
1YML; -.
1YS0; -.
2A2K; -.
2IFD; -.
2IFV; -.
2UZQ; -.
DIP
DIP:323N; -.
IntAct
P30305; -.
PhosphoSite
P30305; -.
Ensembl
ENSG00000101224; Homo sapiens.
GeneID
994; -.
KEGG
hsa:994; -.
H-InvDB
HIX0015603; -.
HGNC
HGNC:1726; CDC25B.
HPA
CAB002663; -.
MIM
116949; gene.
PharmGKB
PA26260; -.
HOVERGEN
P30305; -.
Reactome
REACT_152; Cell Cycle, Mitotic.
NextBio
4170; -.
ArrayExpress
P30305; -.
CleanEx
HS_CDC25B; -.
GermOnline
ENSG00000101224; Homo sapiens.
GO
GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
GO:0005829; C:cytosol; EXP:Reactome.
GO:0005654; C:nucleoplasm; EXP:Reactome.
GO:0005515; F:protein binding; IPI:IntAct.
GO:0004725; F:protein tyrosine phosphatase activity; TAS:UniProtKB.
GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO:0007067; P:mitosis; TAS:ProtInc.
GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO:0006470; P:protein amino acid dephosphorylation; IEA:InterPro.
InterPro
IPR000751; MPI_Phosphatase.
IPR001763; Rhodanese-like.
Gene3D
G3DSA:3.40.250.10; Rhodanese-like; 1.
PANTHER
PTHR10828; MPI_Phosphatase; 1.
Pfam
PF06617; M-inducer_phosp; 1.
PF00581; Rhodanese; 1.
PRINTS
PR00716; MPIPHPHTASE.
SMART
SM00450; RHOD; 1.
PROSITE
PS50206; RHODANESE_3; 1.
Protein Existence
1: Evidence at protein level;
Keywords
3D-structure; Alternative splicing; Cell cycle; Cell division; Hydrolase; Mitosis; Phosphoprotein; Polymorphism; Protein phosphatase;
CHAIN: 1 580, M-phase inducer phosphatase 2. /FTId=PRO_0000198644. DOMAIN: 431 538, Rhodanese. ACT_SITE: 487 487, VAR_SEQ: 68 81, Missing (in isoform 1 and isoform 4). /FTId=VSP_000861. VAR_SEQ: 154 194, Missing (in isoform 2). /FTId=VSP_000862. VAR_SEQ: 194 194, N -> NVRFWKAGVGALREEEGACWGGSLACEDPPLPSWLQ (in isoform 4). /FTId=VSP_012587. VARIANT: 548 548, E -> K (in dbSNP:rs11570019). /FTId=VAR_020933. CONFLICT: 575 575, S -> D (in Ref. 2; AAB21139). STRAND: 396 399, STRAND: 432 439, STRAND: 479 486, STRAND: 519 522, STRAND: 537 540, HELIX: 417 424, HELIX: 443 447, HELIX: 460 468, HELIX: 493 507, HELIX: 525 529, HELIX: 534 536, HELIX: 548 550, HELIX: 551 558, TURN: 425 431, TURN: 530 532, CHAIN: 1 580, M-phase inducer phosphatase 2. /FTId=PRO_0000198644. DOMAIN: 431 538, Rhodanese. ACT_SITE: 487 487, VAR_SEQ: 68 81, Missing (in isoform 1 and isoform 4). /FTId=VSP_000861. VAR_SEQ: 154 194, Missing (in isoform 2). /FTId=VSP_000862. VAR_SEQ: 194 194, N -> NVRFWKAGVGALREEEGACWGGSLACEDPPLPSWLQ (in isoform 4). /FTId=VSP_012587. VARIANT: 548 548, E -> K (in dbSNP:rs11570019). /FTId=VAR_020933. CONFLICT: 575 575, S -> D (in Ref. 2; AAB21139). STRAND: 396 399, HELIX: 417 424, TURN: 425 431, STRAND: 432 439, HELIX: 443 447, HELIX: 460 468, STRAND: 479 486, HELIX: 493 507, STRAND: 519 522, HELIX: 525 529, TURN: 530 532, HELIX: 534 536, STRAND: 537 540, HELIX: 548 550, HELIX: 551 558,
Key Begin End Length Description RESID
  CHAIN 1 580 580 M-phase inducer phosphatase 2. /FTId=PRO_0000198644.
  DOMAIN 431 538 108 Rhodanese.
  ACT_SITE 487 487 1 RESID:AA0005; RESID:AA0171; RESID:AA0269
  VAR_SEQ 68 81 14 Missing (in isoform 1 and isoform 4). /FTId=VSP_000861.
  VAR_SEQ 154 194 41 Missing (in isoform 2). /FTId=VSP_000862.
  VAR_SEQ 194 194 1 N -> NVRFWKAGVGALREEEGACWGGSLACEDPPLPSWLQ (in isoform 4). /FTId=VSP_012587.
  VARIANT 548 548 1 E -> K (in dbSNP:rs11570019). /FTId=VAR_020933.
  CONFLICT 575 575 1 S -> D (in Ref. 2; AAB21139).
  STRAND 396 399 4
  HELIX 417 424 8
  TURN 425 431 7
  STRAND 432 439 8
  HELIX 443 447 5
  HELIX 460 468 9
  STRAND 479 486 8
  HELIX 493 507 15
  STRAND 519 522 4
  HELIX 525 529 5
  TURN 530 532 3
  HELIX 534 536 3
  STRAND 537 540 4
  HELIX 548 550 3
  HELIX 551 558 8


IPI crosslinks:
SP P30305-1 IPI00291990 B4DIG0; ENSP00000245960; REVIEWED:NP_068659; HIT000053659; AAH06395;AAH09953;AAH51711;CAI18847; 1726,CDC25B; 994,CDC25B; UPI000012F474 Hs.153752; CCDS13067.1; GI:11641413; OTTHUMP00000030139;
IPI gene crosslinks:
20 3724401 3734757 1 20p13 ENSG00000101224 1726,CDC25B 994,CDC25B IPI00216511;IPI00291990;IPI00291992;IPI00002089;IPI00029734; P30305-1;P30305-2;P30305-3;P30305-4; B3KS38;B4DIG0;B4DRC3;O43550;Q6MZW8;Q7LDQ7; ENSP00000245960;ENSP00000339125;ENSP00000339170;ENSP00000368918; REVIEWED:NP_004349;REVIEWED:NP_068658;REVIEWED:NP_068659; HIT000053659; Hs.153752; CCDS13065.1;CCDS13066.1;CCDS13067.1; GI:11641411;GI:11641413;GI:4757950; OTTHUMG00000031764; OTTHUMP00000030137;OTTHUMP00000030138;OTTHUMP00000030139;