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P30305

- MPIP2_HUMAN

UniProt

P30305 - MPIP2_HUMAN

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Protein

M-phase inducer phosphatase 2

Gene

CDC25B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei487 – 4871

GO - Molecular functioni

  1. protein kinase binding Source: UniProtKB
  2. protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. female meiosis I Source: Ensembl
  2. G2/M transition of mitotic cell cycle Source: UniProtKB
  3. mitotic cell cycle Source: UniProtKB
  4. mitotic nuclear division Source: ProtInc
  5. oocyte maturation Source: Ensembl
  6. peptidyl-tyrosine dephosphorylation Source: GOC
  7. positive regulation of cell proliferation Source: ProtInc
  8. positive regulation of cytokinesis Source: UniProtKB
  9. positive regulation of mitotic cell cycle Source: UniProtKB
  10. positive regulation of protein kinase activity Source: Ensembl
  11. protein phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

BRENDAi3.1.3.48. 2681.
ReactomeiREACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_2101. Cyclin B2 mediated events.
REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:1726. CDC25B.

Subcellular locationi

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. nucleoplasm Source: Reactome
  5. nucleus Source: HPA
  6. spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26260.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 580580M-phase inducer phosphatase 2PRO_0000198644Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei169 – 1691Phosphoserine; by MELK1 Publication
Modified residuei249 – 2491Phosphoserine1 Publication
Modified residuei323 – 3231Phosphoserine; by MELK and MAPK143 Publications
Modified residuei353 – 3531Phosphoserine; by AURKA1 Publication
Modified residuei375 – 3751Phosphoserine; by BRSK1 and MAPK142 Publications

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.9 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP30305.
PaxDbiP30305.
PRIDEiP30305.

PTM databases

PhosphoSiteiP30305.

Expressioni

Gene expression databases

BgeeiP30305.
CleanExiHS_CDC25B.
ExpressionAtlasiP30305. baseline and differential.
GenevestigatoriP30305.

Organism-specific databases

HPAiCAB002663.
HPA038892.
HPA038893.

Interactioni

Subunit structurei

Interacts with MAPK14 and 14-3-3 proteins.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
YWHABP319464EBI-1051746,EBI-359815
YWHAHQ049173EBI-1051746,EBI-306940
YWHAZP631044EBI-1051746,EBI-347088

Protein-protein interaction databases

BioGridi107429. 30 interactions.
DIPiDIP-323N.
IntActiP30305. 8 interactions.
MINTiMINT-124404.
STRINGi9606.ENSP00000245960.

Structurei

Secondary structure

1
580
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi396 – 3994
Helixi417 – 4248
Turni425 – 4317
Beta strandi432 – 4398
Helixi443 – 4475
Helixi460 – 4689
Turni469 – 4713
Beta strandi480 – 4867
Beta strandi488 – 4925
Helixi493 – 50715
Beta strandi519 – 5224
Helixi525 – 5295
Turni530 – 5323
Helixi534 – 5363
Beta strandi537 – 5404
Helixi548 – 5503
Helixi551 – 5588

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CWRX-ray2.10A370-580[»]
1CWSX-ray2.00A370-580[»]
1CWTX-ray2.30A388-565[»]
1QB0X-ray1.91A370-580[»]
1YM9X-ray2.00A391-564[»]
1YMDX-ray1.70A391-564[»]
1YMKX-ray1.70A391-564[»]
1YMLX-ray1.70A391-564[»]
1YS0X-ray2.00A391-564[»]
2A2KX-ray1.52A391-564[»]
2IFDX-ray2.00A391-564[»]
2IFVX-ray1.60A391-564[»]
2UZQX-ray2.38A/B/C/D/E/F391-580[»]
3FQTX-ray1.80C38-46[»]
3FQUX-ray1.80C38-46[»]
ProteinModelPortaliP30305.
SMRiP30305. Positions 388-564.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30305.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini431 – 538108RhodanesePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the MPI phosphatase family.Curated
Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5105.
GeneTreeiENSGT00390000018747.
HOVERGENiHBG052501.
InParanoidiP30305.
KOiK05866.
OMAiTPKSQVG.
OrthoDBiEOG7288R1.
PhylomeDBiP30305.
TreeFamiTF101056.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PfamiPF06617. M-inducer_phosp. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSiPR00716. MPIPHPHTASE.
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 3 (identifier: P30305) [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.

« Hide

        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
Length:580
Mass (Da):64,987
Last modified:May 27, 2002 - v2
Checksum:iEDE24B0E84AC1BE3
GO
Isoform 1 (identifier: P30305-2) [UniParc]FASTAAdd to Basket

Also known as: CDC25B1

The sequence of this isoform differs from the canonical sequence as follows:
     68-81: Missing.

Show »
Length:566
Mass (Da):63,443
Checksum:i7C54E3E799ECDA50
GO
Isoform 2 (identifier: P30305-3) [UniParc]FASTAAdd to Basket

Also known as: CDC25B2

The sequence of this isoform differs from the canonical sequence as follows:
     154-194: Missing.

Show »
Length:539
Mass (Da):60,756
Checksum:iCDA92929F8183BE9
GO
Isoform 4 (identifier: P30305-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     68-81: Missing.
     194-194: N → NVRFWKAGVGALREEEGACWGGSLACEDPPLPSWLQ

Note: No experimental confirmation available.

Show »
Length:601
Mass (Da):67,241
Checksum:i8E32AEC15A3845D7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti575 – 5751S → D in AAB21139. (PubMed:1662986)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti548 – 5481E → K.1 Publication
Corresponds to variant rs11570019 [ dbSNP | Ensembl ].
VAR_020933

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei68 – 8114Missing in isoform 1 and isoform 4. 2 PublicationsVSP_000861Add
BLAST
Alternative sequencei154 – 19441Missing in isoform 2. 1 PublicationVSP_000862Add
BLAST
Alternative sequencei194 – 1941N → NVRFWKAGVGALREEEGACW GGSLACEDPPLPSWLQ in isoform 4. CuratedVSP_012587

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSiCCDS13065.1. [P30305-2]
CCDS13066.1. [P30305-3]
CCDS13067.1. [P30305-1]
PIRiB41648.
RefSeqiNP_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]
UniGeneiHs.153752.

Genome annotation databases

EnsembliENST00000245960; ENSP00000245960; ENSG00000101224. [P30305-1]
ENST00000340833; ENSP00000339170; ENSG00000101224. [P30305-3]
ENST00000439880; ENSP00000405972; ENSG00000101224. [P30305-2]
GeneIDi994.
KEGGihsa:994.
UCSCiuc002wjl.3. human. [P30305-1]
uc002wjo.3. human. [P30305-2]
uc002wjp.3. human. [P30305-3]

Polymorphism databases

DMDMi21264471.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P30305.
SMRi P30305. Positions 388-564.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107429. 30 interactions.
DIPi DIP-323N.
IntActi P30305. 8 interactions.
MINTi MINT-124404.
STRINGi 9606.ENSP00000245960.

Chemistry

BindingDBi P30305.
ChEMBLi CHEMBL4804.

PTM databases

PhosphoSitei P30305.

Polymorphism databases

DMDMi 21264471.

Proteomic databases

MaxQBi P30305.
PaxDbi P30305.
PRIDEi P30305.

Protocols and materials databases

DNASUi 994.
Structural Biology Knowledgebase Search...

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 uc002wjl.3. human. [P30305-1 ]
uc002wjo.3. human. [P30305-2 ]
uc002wjp.3. human. [P30305-3 ]

Organism-specific databases

CTDi 994.
GeneCardsi GC20P003771.
HGNCi HGNC:1726. CDC25B.
HPAi CAB002663.
HPA038892.
HPA038893.
MIMi 116949. gene.
neXtProti NX_P30305.
PharmGKBi PA26260.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5105.
GeneTreei ENSGT00390000018747.
HOVERGENi HBG052501.
InParanoidi P30305.
KOi K05866.
OMAi TPKSQVG.
OrthoDBi EOG7288R1.
PhylomeDBi P30305.
TreeFami TF101056.

Enzyme and pathway databases

BRENDAi 3.1.3.48. 2681.
Reactomei REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_2101. Cyclin B2 mediated events.
REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.

Miscellaneous databases

EvolutionaryTracei P30305.
GeneWikii CDC25B.
GenomeRNAii 994.
NextBioi 4170.
PROi P30305.
SOURCEi Search...

Gene expression databases

Bgeei P30305.
CleanExi HS_CDC25B.
ExpressionAtlasi P30305. baseline and differential.
Genevestigatori P30305.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
InterProi IPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view ]
Pfami PF06617. M-inducer_phosp. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view ]
PRINTSi PR00716. MPIPHPHTASE.
SMARTi SM00450. RHOD. 1 hit.
[Graphical view ]
SUPFAMi SSF52821. SSF52821. 1 hit.
PROSITEi PS50206. RHODANESE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Specific activation of cdc25 tyrosine phosphatases by B-type cyclins: evidence for multiple roles of mitotic cyclins."
    Galaktionov K.I., Beach D.
    Cell 67:1181-1194(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "An additional homolog of the fission yeast cdc25+ gene occurs in humans and is highly expressed in some cancer cells."
    Nagata A., Igarashi M., Jinno S., Suto K., Okayama H.
    New Biol. 3:959-968(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Alternative splicing of the human CDC25B tyrosine phosphatase. Possible implications for growth control?"
    Baldin V., Cans C., Superti-Furga G., Docommun B.
    Oncogene 14:2485-2495(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3).
  4. NIEHS SNPs program
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-548.
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    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.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  8. "Alternative splicing of cdc25B."
    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.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-352 (ISOFORMS 2 AND 3).
  9. "Initiation of a G2/M checkpoint after ultraviolet radiation requires p38 kinase."
    Bulavin D.V., Higashimoto Y., Popoff I.J., Gaarde W.A., Basrur V., Potapova O., Appella E., Fornace A.J. Jr.
    Nature 411:102-107(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-323 AND SER-375, INTERACTION WITH MAPK14 AND 14-3-3 PROTEINS.
  10. "Human pEg3 kinase associates with and phosphorylates CDC25B phosphatase: a potential role for pEg3 in cell cycle regulation."
    Davezac N., Baldin V., Blot J., Ducommun B., Tassan J.P.
    Oncogene 21:7630-7641(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-323.
  11. "Human SAD1 kinase is involved in UV-induced DNA damage checkpoint function."
    Lu R., Niida H., Nakanishi M.
    J. Biol. Chem. 279:31164-31170(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-375.
    Tissue: Testis.
  12. Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-353 BY AURKA.
  13. "Centrosome-associated Chk1 prevents premature activation of cyclin-B-Cdk1 kinase."
    Kraemer A., Mailand N., Lukas C., Syljuaesen R.G., Wilkinson C.J., Nigg E.A., Bartek J., Lukas J.
    Nat. Cell Biol. 6:884-891(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION BY CHEK1.
  14. "CDC25B phosphorylated by pEg3 localizes to the centrosome and the spindle poles at mitosis."
    Mirey G., Chartrain I., Froment C., Quaranta M., Bouche J.P., Monsarrat B., Tassan J.P., Ducommun B.
    Cell Cycle 4:806-811(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-169, SUBCELLULAR LOCATION.
  15. "MAPKAP kinase-2 is a cell cycle checkpoint kinase that regulates the G2/M transition and S phase progression in response to UV irradiation."
    Manke I.A., Nguyen A., Lim D., Stewart M.Q., Elia A.E., Yaffe M.B.
    Mol. Cell 17:37-48(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-323 BY MAPKAPK2.
  16. "Rho GTPases regulate PRK2/PKN2 to control entry into mitosis and exit from cytokinesis."
    Schmidt A., Durgan J., Magalhaes A., Hall A.
    EMBO J. 26:1624-1636(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Crystal structure of the catalytic subunit of Cdc25B required for G2/M phase transition of the cell cycle."
    Reynolds R.A., Yem A.W., Wolfe C.L., Deibel M.R. Jr., Chidester C.G., Watenpaugh K.D.
    J. Mol. Biol. 293:559-568(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 370-580.

Entry informationi

Entry nameiMPIP2_HUMAN
AccessioniPrimary (citable) accession number: P30305
Secondary accession number(s): D3DVY1
, D3DVY2, D3DVY3, D3DVY4, O43551, Q13971, Q5JX77, Q6RSS1, Q9BRA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 27, 2002
Last modified: October 29, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3