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P30305 (MPIP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
M-phase inducer phosphatase 2

EC=3.1.3.48
Alternative name(s):
Dual specificity phosphatase Cdc25B
Gene names
Name:CDC25B
Synonyms:CDC25HU2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length580 AA.
Sequence statusComplete.
Protein existenceEvidence 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.16

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

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle pole Ref.12 Ref.13 Ref.14.

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 Ref.16

Sequence similarities

Belongs to the MPI phosphatase family.

Contains 1 rhodanese domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement Ref.10. Source: UniProtKB

female meiosis I

Inferred from electronic annotation. Source: Ensembl

mitosis

Traceable author statement Ref.1. Source: ProtInc

mitotic cell cycle

Traceable author statement Ref.3. Source: UniProtKB

oocyte maturation

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine dephosphorylation

Traceable author statement Ref.1Ref.3. Source: GOC

positive regulation of cell proliferation

Traceable author statement PubMed 8276402. Source: ProtInc

positive regulation of cytokinesis

Inferred from mutant phenotype Ref.16. Source: UniProtKB

positive regulation of mitotic cell cycle

Inferred from mutant phenotype Ref.16. Source: UniProtKB

positive regulation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay Ref.16. Source: UniProtKB

   Cellular_componentcentrosome

Inferred from direct assay Ref.14. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

spindle pole

Inferred from direct assay Ref.14. Source: UniProtKB

   Molecular_functionprotein kinase binding

Inferred from physical interaction Ref.10Ref.14. Source: UniProtKB

protein tyrosine phosphatase activity

Traceable author statement Ref.3. Source: UniProtKB

Complete GO annotation...

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 580580M-phase inducer phosphatase 2
PRO_0000198644

Regions

Domain431 – 538108Rhodanese

Sites

Active site4871

Amino acid modifications

Modified residue1691Phosphoserine; by MELK Ref.14
Modified residue2491Phosphoserine Ref.18
Modified residue3231Phosphoserine; by MELK and MAPK14 Ref.9 Ref.10 Ref.15
Modified residue3531Phosphoserine; by AURKA Ref.12
Modified residue3751Phosphoserine; by BRSK1 and MAPK14 Ref.9 Ref.11

Natural variations

Alternative sequence68 – 8114Missing in isoform 1 and isoform 4.
VSP_000861
Alternative sequence154 – 19441Missing in isoform 2.
VSP_000862
Alternative sequence1941N → NVRFWKAGVGALREEEGACW GGSLACEDPPLPSWLQ in isoform 4.
VSP_012587
Natural variant5481E → K. Ref.4
Corresponds to variant rs11570019 [ dbSNP | Ensembl ].
VAR_020933

Experimental info

Sequence conflict5751S → D in AAB21139. Ref.2

Secondary structure

............................ 580
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 (CDC25B3) [UniParc].

Last modified May 27, 2002. Version 2.
Checksum: EDE24B0E84AC1BE3

FASTA58064,987
        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 

« Hide

Isoform 1 (CDC25B1) [UniParc].

Checksum: 7C54E3E799ECDA50
Show »

FASTA56663,443
Isoform 2 (CDC25B2) [UniParc].

Checksum: CDA92929F8183BE9
Show »

FASTA53960,756
Isoform 4 [UniParc].

Checksum: 8E32AEC15A3845D7
Show »

FASTA60167,241

References

« Hide '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] [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. expand/collapse author list , 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]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. expand/collapse author list , 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] [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]"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] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

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.
PIRB41648.
RefSeqNP_001274448.1. NM_001287519.1.
NP_001274453.1. NM_001287524.1.
NP_004349.1. NM_004358.4.
NP_068658.1. NM_021872.3.
NP_068659.1. NM_021873.3.
UniGeneHs.153752.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP30305.
SMRP30305. Positions 388-564.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107429. 30 interactions.
DIPDIP-323N.
IntActP30305. 8 interactions.
MINTMINT-124404.
STRING9606.ENSP00000245960.

Chemistry

BindingDBP30305.
ChEMBLCHEMBL4804.

PTM databases

PhosphoSiteP30305.

Polymorphism databases

DMDM21264471.

Proteomic databases

PaxDbP30305.
PRIDEP30305.

Protocols and materials databases

DNASU994.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000245960; ENSP00000245960; ENSG00000101224. [P30305-1]
ENST00000340833; ENSP00000339170; ENSG00000101224. [P30305-3]
ENST00000439880; ENSP00000405972; ENSG00000101224. [P30305-2]
GeneID994.
KEGGhsa:994.
UCSCuc002wjl.3. human. [P30305-1]
uc002wjo.3. human. [P30305-2]
uc002wjp.3. human. [P30305-3]

Organism-specific databases

CTD994.
GeneCardsGC20P003771.
HGNCHGNC:1726. CDC25B.
HPACAB002663.
HPA038892.
HPA038893.
MIM116949. gene.
neXtProtNX_P30305.
PharmGKBPA26260.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5105.
HOVERGENHBG052501.
InParanoidP30305.
KOK05866.
OMATPKSQVG.
OrthoDBEOG7288R1.
PhylomeDBP30305.
TreeFamTF101056.

Enzyme and pathway databases

BRENDA3.1.3.48. 2681.
ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressP30305.
BgeeP30305.
CleanExHS_CDC25B.
GenevestigatorP30305.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
InterProIPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PfamPF06617. M-inducer_phosp. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSPR00716. MPIPHPHTASE.
SMARTSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF52821. SSF52821. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP30305.
GeneWikiCDC25B.
GenomeRNAi994.
NextBio4170.
PROP30305.
SOURCESearch...

Entry information

Entry nameMPIP2_HUMAN
AccessionPrimary (citable) accession number: P30305
Secondary accession number(s): D3DVY1 expand/collapse secondary AC list , 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: April 16, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM