P30305 (MPIP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
M-phase inducer phosphatase 2
EC=3.1.3.48

Alternative name(s):
Dual specificity phosphatase Cdc25B

Gene names

Name:	CDC25B
Synonyms:	CDC25HU2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	580 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.15
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Enzyme regulation	Stimulated by B-type cyclins.
Subunit structure	Interacts with MAPK14 and 14-3-3 proteins. Ref.9
Subcellular location	Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle pole Ref.11 Ref.12 Ref.13.
Post-translational modification	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. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
Sequence similarities	Belongs to the MPI phosphatase family. Contains 1 rhodanese domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	G2/M transition of mitotic cell cycle Traceable author statement Ref.10. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Traceable author statement. Source: ProtInc positive regulation of cell proliferation Traceable author statement. Source: ProtInc
Cellular component	centrosome Inferred from direct assay Ref.13. Source: UniProtKB cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome spindle pole Inferred from direct assay Ref.13. Source: UniProtKB
Molecular function	protein kinase binding Inferred from physical interaction Ref.10Ref.13. Source: UniProtKB protein tyrosine phosphatase activity Traceable author statement Ref.3. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 3 (identifier: P30305-1)

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.

Isoform 1 (identifier: P30305-2)

Also known as: CDC25B1;

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

Isoform 2 (identifier: P30305-3)

Also known as: CDC25B2;

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

Isoform 4 (identifier: P30305-4)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 580

580

M-phase inducer phosphatase 2

PRO_0000198644

Regions

Domain

431 – 538

108

Rhodanese

Sites

Active site

487

1

Amino acid modifications

Modified residue

169

1

Phosphoserine; by MELK Ref.13

Modified residue

323

1

Phosphoserine; by MELK and MAPK14 Ref.9 Ref.10 Ref.14

Modified residue

353

1

Phosphoserine; by AURKA Ref.11

Modified residue

375

1

Phosphoserine; by MAPK14 Ref.9

Natural variations

Alternative sequence

68 – 81

14

Missing in isoform 1 and isoform 4.

VSP_000861

Alternative sequence

154 – 194

41

Missing in isoform 2.

VSP_000862

Alternative sequence

194

1

N → NVRFWKAGVGALREEEGACW GGSLACEDPPLPSWLQ in isoform 4.

VSP_012587

Natural variant

548

1

E → K. Ref.4
Corresponds to variant rs11570019 [ dbSNP | Ensembl ].

VAR_020933

Experimental info

Sequence conflict

575

1

S → D in AAB21139. Ref.2

Secondary structure

1

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580

Helix Strand Turn

Details...

Beta strand

396 – 399

4

Helix

417 – 424

8

Turn

425 – 431

7

Beta strand

432 – 439

8

Helix

443 – 447

5

Helix

460 – 468

9

Beta strand

479 – 486

8

Helix

493 – 507

15

Beta strand

519 – 522

4

Helix

525 – 529

5

Turn

530 – 532

3

Helix

534 – 536

3

Beta strand

537 – 540

4

Helix

548 – 550

3

Helix

551 – 558

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 3 (CDC25B3) [UniParc]. Last modified May 27, 2002. Version 2. Checksum: EDE24B0E84AC1BE3	FASTA	580	64,987
	10 20 30 40 50 60 MEVPQPEPAP GSALSPAGVC GGAQRPGHLP GLLLGSHGLL GSPVRAAASS PVTTLTQTMH 70 80 90 100 110 120 DLAGLGSETP KSQVGTLLFR SRSRLTHLSL SRRASESSLS SESSESSDAG LCMDSPSPMD 130 140 150 160 170 180 PHMAEQTFEQ AIQAASRIIR NEQFAIRRFQ SMPVRLLGHS PVLRNITNSQ APDGRRKSEA 190 200 210 220 230 240 GSGAASSSGE DKENDGFVFK MPWKPTHPSS THALAEWASR REAFAQRPSS APDLMCLSPD 250 260 270 280 290 300 RKMEVEELSP LALGRFSLTP AEGDTEEDDG FVDILESDLK DDDAVPPGME SLISAPLVKT 310 320 330 340 350 360 LEKEEEKDLV MYSKCQRLFR SPSMPCSVIR PILKRLERPQ DRDTPVQNKR RRSVTPPEEQ 370 380 390 400 410 420 QEAEEPKARV LRSKSLCHDE IENLLDSDHR ELIGDYSKAF LLQTVDGKHQ DLKYISPETM 430 440 450 460 470 480 VALLTGKFSN IVDKFVIVDC RYPYEYEGGH IKTAVNLPLE RDAESFLLKS PIAPCSLDKR 490 500 510 520 530 540 VILIFHCEFS SERGPRMCRF IRERDRAVND YPSLYYPEMY ILKGGYKEFF PQHPNFCEPQ 550 560 570 580 DYRPMNHEAF KDELKTFRLK TRSWAGERSR RELCSRLQDQ
	Isoform 1 (CDC25B1) [UniParc]. Checksum: 7C54E3E799ECDA50	FASTA	566	63,443
	10 20 30 40 50 60 MEVPQPEPAP GSALSPAGVC GGAQRPGHLP GLLLGSHGLL GSPVRAAASS PVTTLTQTMH 70 80 90 100 110 120 DLAGLGSRSR LTHLSLSRRA SESSLSSESS ESSDAGLCMD SPSPMDPHMA EQTFEQAIQA 130 140 150 160 170 180 ASRIIRNEQF AIRRFQSMPV RLLGHSPVLR NITNSQAPDG RRKSEAGSGA ASSSGEDKEN 190 200 210 220 230 240 DGFVFKMPWK PTHPSSTHAL AEWASRREAF AQRPSSAPDL MCLSPDRKME VEELSPLALG 250 260 270 280 290 300 RFSLTPAEGD TEEDDGFVDI LESDLKDDDA VPPGMESLIS APLVKTLEKE EEKDLVMYSK 310 320 330 340 350 360 CQRLFRSPSM PCSVIRPILK RLERPQDRDT PVQNKRRRSV TPPEEQQEAE EPKARVLRSK 370 380 390 400 410 420 SLCHDEIENL LDSDHRELIG DYSKAFLLQT VDGKHQDLKY ISPETMVALL TGKFSNIVDK 430 440 450 460 470 480 FVIVDCRYPY EYEGGHIKTA VNLPLERDAE SFLLKSPIAP CSLDKRVILI FHCEFSSERG 490 500 510 520 530 540 PRMCRFIRER DRAVNDYPSL YYPEMYILKG GYKEFFPQHP NFCEPQDYRP MNHEAFKDEL 550 560 KTFRLKTRSW AGERSRRELC SRLQDQ
	Isoform 2 (CDC25B2) [UniParc]. Checksum: CDA92929F8183BE9	FASTA	539	60,756
	10 20 30 40 50 60 MEVPQPEPAP GSALSPAGVC GGAQRPGHLP GLLLGSHGLL GSPVRAAASS PVTTLTQTMH 70 80 90 100 110 120 DLAGLGSETP KSQVGTLLFR SRSRLTHLSL SRRASESSLS SESSESSDAG LCMDSPSPMD 130 140 150 160 170 180 PHMAEQTFEQ AIQAASRIIR NEQFAIRRFQ SMPDGFVFKM PWKPTHPSST HALAEWASRR 190 200 210 220 230 240 EAFAQRPSSA PDLMCLSPDR KMEVEELSPL ALGRFSLTPA EGDTEEDDGF VDILESDLKD 250 260 270 280 290 300 DDAVPPGMES LISAPLVKTL EKEEEKDLVM YSKCQRLFRS PSMPCSVIRP ILKRLERPQD 310 320 330 340 350 360 RDTPVQNKRR RSVTPPEEQQ EAEEPKARVL RSKSLCHDEI ENLLDSDHRE LIGDYSKAFL 370 380 390 400 410 420 LQTVDGKHQD LKYISPETMV ALLTGKFSNI VDKFVIVDCR YPYEYEGGHI KTAVNLPLER 430 440 450 460 470 480 DAESFLLKSP IAPCSLDKRV ILIFHCEFSS ERGPRMCRFI RERDRAVNDY PSLYYPEMYI 490 500 510 520 530 LKGGYKEFFP QHPNFCEPQD YRPMNHEAFK DELKTFRLKT RSWAGERSRR ELCSRLQDQ
	Isoform 4 [UniParc]. Checksum: 8E32AEC15A3845D7	FASTA	601	67,241
	10 20 30 40 50 60 MEVPQPEPAP GSALSPAGVC GGAQRPGHLP GLLLGSHGLL GSPVRAAASS PVTTLTQTMH 70 80 90 100 110 120 DLAGLGSRSR LTHLSLSRRA SESSLSSESS ESSDAGLCMD SPSPMDPHMA EQTFEQAIQA 130 140 150 160 170 180 ASRIIRNEQF AIRRFQSMPV RLLGHSPVLR NITNSQAPDG RRKSEAGSGA ASSSGEDKEN 190 200 210 220 230 240 VRFWKAGVGA LREEEGACWG GSLACEDPPL PSWLQDGFVF KMPWKPTHPS STHALAEWAS 250 260 270 280 290 300 RREAFAQRPS SAPDLMCLSP DRKMEVEELS PLALGRFSLT PAEGDTEEDD GFVDILESDL 310 320 330 340 350 360 KDDDAVPPGM ESLISAPLVK TLEKEEEKDL VMYSKCQRLF RSPSMPCSVI RPILKRLERP 370 380 390 400 410 420 QDRDTPVQNK RRRSVTPPEE QQEAEEPKAR VLRSKSLCHD EIENLLDSDH RELIGDYSKA 430 440 450 460 470 480 FLLQTVDGKH QDLKYISPET MVALLTGKFS NIVDKFVIVD CRYPYEYEGG HIKTAVNLPL 490 500 510 520 530 540 ERDAESFLLK SPIAPCSLDK RVILIFHCEF SSERGPRMCR FIRERDRAVN DYPSLYYPEM 550 560 570 580 590 600 YILKGGYKEF FPQHPNFCEP QDYRPMNHEA FKDELKTFRL KTRSWAGERS RRELCSRLQD Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1836978] [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: 1662986] [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: 9188863] [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: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [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: 11333986] [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: 12400006] [Abstract] Cited for: PHOSPHORYLATION AT SER-323.
[11]	"Phosphorylation of CDC25B by Aurora-A at the centrosome contributes to the G2-M transition." Dutertre S., Cazales M., Quaranta M., Froment C., Trabut V., Dozier C., Mirey G., Bouche J.P., Theis-Febvre N., Schmitt E., Monsarrat B., Prigent C., Ducommun B. J. Cell Sci. 117:2523-2531(2004) [PubMed: 15128871] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-353 BY AURKA.
[12]	"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: 15311285] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION BY CHEK1.
[13]	"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: 15908796] [Abstract] Cited for: PHOSPHORYLATION AT SER-169, SUBCELLULAR LOCATION.
[14]	"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: 15629715] [Abstract] Cited for: PHOSPHORYLATION AT SER-323 BY MAPKAPK2.
[15]	"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: 17332740] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION.
[16]	"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: 10543950] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 370-580.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00029734.
IPI00216511.
IPI00291990.
IPI00291992.

PIR

B41648.

RefSeq

NP_004349.1. NM_004358.3.
NP_068658.1. NM_021872.2.
NP_068659.1. NM_021873.2.

UniGene

Hs.153752.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P30305.

SMR

P30305. Positions 388-564.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-323N.

IntAct

P30305. 4 interactions.

MINT

MINT-124404.

STRING

P30305.

PTM databases

PhosphoSite

P30305.

Polymorphism databases

DMDM

21264471.

Proteomic databases

PRIDE

P30305.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000245960; ENSP00000245960; ENSG00000101224.

GeneID

994.

KEGG

hsa:994.

UCSC

uc002wjn.1. human.
uc002wjo.1. human.
uc002wjp.1. human.

Organism-specific databases

CTD

994.

GeneCards

GC20P003771.

H-InvDB

HIX0015603.

HGNC

HGNC:1726. CDC25B.

HPA

CAB002663.

MIM

116949. gene.

neXtProt

NX_P30305.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000018747.

HOVERGEN

HBG052501.

InParanoid

P30305.

OMA

HRELIGD.

OrthoDB

EOG408N87.

Enzyme and pathway databases

BRENDA

3.1.3.48. 2681.

Pathway_Interaction_DB

aurora_a_pathway. Aurora A signaling.
foxm1pathway. FOXM1 transcription factor network.
p38_mk2pathway. p38 signaling mediated by MAPKAP kinases.

Reactome

REACT_152. Cell Cycle, Mitotic.

Gene expression databases

ArrayExpress

P30305.

Bgee

P30305.

CleanEx

HS_CDC25B.

Genevestigator

P30305.

GermOnline

ENSG00000101224. Homo sapiens.

Family and domain databases

InterPro

IPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like.
[Graphical view]

Gene3D

G3DSA:3.40.250.10. Rhodanese-like. 1 hit.

KO

K05866.

PANTHER

PTHR10828. MPI_Phosphatase. 1 hit.

Pfam

PF06617. M-inducer_phosp. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]

PRINTS

PR00716. MPIPHPHTASE.

SMART

SM00450. RHOD. 1 hit.
[Graphical view]

SUPFAM

SSF52821. Rhodanese-like. 1 hit.

PROSITE

PS50206. RHODANESE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

4170.

SOURCE

Search...

Entry information

Entry name

MPIP2_HUMAN

Accession

Primary (citable) accession number: P30305
Secondary accession number(s): D3DVY1 , D3DVY2, D3DVY3, D3DVY4, O43551, Q13971, Q5JX77, Q6RSS1, Q9BRA6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	May 27, 2002
Last modified:	January 25, 2012
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

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.