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P30307 (MPIP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. 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 3

EC=3.1.3.48
Alternative name(s):
Dual specificity phosphatase Cdc25C
Gene names
Name:CDC25C
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle. When phosphorylated, highly effective in activating G2 cells into prophase. Directly dephosphorylates CDK1 and activates its kinase activity. Ref.8

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Interacts with HIV-1 Vpr, thereby inactivating CDC25C phosphatase activity. Interacts with MAPK14 and 14-3-3 proteins. When phosphorylated on Ser-129 and/or Thr-130, interacts with PLK1. Ref.11 Ref.12 Ref.15

Subcellular location

Nucleus Ref.8 Ref.14.

Developmental stage

Expressed predominantly in G2 phase.

Post-translational modification

Phosphorylated by CHEK1 and MAPK14 at Ser-216. This phosphorylation creates a binding site for 14-3-3 protein and inhibits the phosphatase. Phosphorylated by PLK4. Phosphorylated by PLK1, leading to activate the phosphatase activity. Phosphorylation by PLK3 at Ser-191 promotes nuclear translocation. Ser-198 is a minor phosphorylation site. Was initially reported to be phosphorylated by PLK3 at Ser-216 (Ref.9). However, such phosphorylation by PLK3 was not confirmed by other groups. Phosphorylation at Thr-48, Thr-67, Ser-122, Thr-130, Ser-168 and Ser-214 occurs at G2 and G2-M transition and is probably catalyzed by CDK1. Ser-168 phosphorylation levels are lower than those at the other 5 CDK1 sites. Phosphorylation by CDK1 leads to increased activity. Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17

Sequence similarities

Belongs to the MPI phosphatase family.

Contains 1 rhodanese domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Host-virus interaction
Mitosis
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Traceable author statement. Source: Reactome

G2/M transition of mitotic cell cycle

Inferred from genetic interaction Ref.1. Source: UniProtKB

cell proliferation

Traceable author statement Ref.6. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

peptidyl-tyrosine dephosphorylation

Non-traceable author statement Ref.2. Source: GOC

regulation of cell cycle

Traceable author statement. Source: Reactome

regulation of cyclin-dependent protein serine/threonine kinase activity

Traceable author statement Ref.6. Source: UniProtKB

regulation of mitosis

Traceable author statement PubMed 1828290. Source: ProtInc

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.14. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionWW domain binding

Inferred from physical interaction PubMed 10037602. Source: BHF-UCL

protein kinase binding

Inferred from physical interaction Ref.14. Source: UniProtKB

protein tyrosine phosphatase activity

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P30307-1)

Also known as: CDC25C1;

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 2 (identifier: P30307-2)

Also known as: CDC25C2;

The sequence of this isoform differs from the canonical sequence as follows:
     124-153: Missing.
Isoform 3 (identifier: P30307-5)

Also known as: CDC25C3;

The sequence of this isoform is not available.
Isoform 4 (identifier: P30307-3)

Also known as: CDC25C4;

The sequence of this isoform differs from the canonical sequence as follows:
     66-123: GTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSP → SPGFFRTSGSAFSWD
Note: Contains a phosphoserine at position 61.
Isoform 5 (identifier: P30307-4)

Also known as: CDC25C5; Cdc25Cdm;

The sequence of this isoform differs from the canonical sequence as follows:
     66-123: GTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSP → SPGFFRTSGSAFSWD
     124-153: Missing.
Note: Contains a phosphoserine at position 61.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.21
Chain2 – 473472M-phase inducer phosphatase 3
PRO_0000198647

Regions

Domain321 – 428108Rhodanese
Region334 – 37946HIV-1 Vpr binding site

Sites

Active site3771 By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.21
Modified residue381Phosphoserine Ref.19
Modified residue481Phosphothreonine Ref.8 Ref.19
Modified residue571Phosphoserine Ref.19
Modified residue611Phosphoserine Ref.18 Ref.19 Ref.20
Modified residue641Phosphoserine Ref.18 Ref.19 Ref.20
Modified residue671Phosphothreonine Ref.8 Ref.19 Ref.20
Modified residue1221Phosphoserine; by CDK1 Probable
Modified residue1291Phosphoserine
Modified residue1301Phosphothreonine; by CDK1 Probable
Modified residue1681Phosphoserine Ref.8 Ref.18
Modified residue1911Phosphoserine; by PLK3 Ref.14
Modified residue1981Phosphoserine; by PLK3 Ref.14
Modified residue2141Phosphoserine; by CDK1 Probable
Modified residue2161Phosphoserine; by CHEK1, CHEK2, BRSK1 and MAPK14 Ref.11 Ref.13 Ref.16
Modified residue4721Phosphoserine Ref.18

Natural variations

Alternative sequence66 – 12358GTPKR…MKCSP → SPGFFRTSGSAFSWD in isoform 4 and isoform 5.
VSP_000863
Alternative sequence124 – 15330Missing in isoform 2 and isoform 5.
VSP_000864
Natural variant141S → N.
Corresponds to variant rs11567959 [ dbSNP | Ensembl ].
VAR_027922
Natural variant701R → C. Ref.1 Ref.5 Ref.6
Corresponds to variant rs3734166 [ dbSNP | Ensembl ].
VAR_027923
Natural variant781S → N.
Corresponds to variant rs11567962 [ dbSNP | Ensembl ].
VAR_027924
Natural variant2971G → R.
Corresponds to variant rs11567997 [ dbSNP | Ensembl ].
VAR_020146

Experimental info

Mutagenesis1291S → V: Loss of phosphorylation. Severely impairs PLK1-binding. Ref.12
Mutagenesis1301T → A: Loss of phosphorylation. Severely impairs PLK1-binding. Ref.12
Mutagenesis1911S → A: Facilitates nuclear exclusion. Ref.14
Mutagenesis1911S → D: Mimicks phosphorylation state, leading to enhanced accumulation in the nucleus. Ref.14
Mutagenesis3521E → K: Partial loss of HIV-1 Vpr binding. Ref.15
Mutagenesis3591K → E: No effect on HIV-1 Vpr binding. Ref.15

Secondary structure

............................... 473
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (CDC25C1) [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 0658A1F1B9B8996A

FASTA47353,365
        10         20         30         40         50         60 
MSTELFSSTR EEGSSGSGPS FRSNQRKMLN LLLERDTSFT VCPDVPRTPV GKFLGDSANL 

        70         80         90        100        110        120 
SILSGGTPKR CLDLSNLSSG EITATQLTTS ADLDETGHLD SSGLQEVHLA GMNHDQHLMK 

       130        140        150        160        170        180 
CSPAQLLCST PNGLDRGHRK RDAMCSSSAN KENDNGNLVD SEMKYLGSPI TTVPKLDKNP 

       190        200        210        220        230        240 
NLGEDQAEEI SDELMEFSLK DQEAKVSRSG LYRSPSMPEN LNRPRLKQVE KFKDNTIPDK 

       250        260        270        280        290        300 
VKKKYFSGQG KLRKGLCLKK TVSLCDITIT QMLEEDSNQG HLIGDFSKVC ALPTVSGKHQ 

       310        320        330        340        350        360 
DLKYVNPETV AALLSGKFQG LIEKFYVIDC RYPYEYLGGH IQGALNLYSQ EELFNFFLKK 

       370        380        390        400        410        420 
PIVPLDTQKR IIIVFHCEFS SERGPRMCRC LREEDRSLNQ YPALYYPELY ILKGGYRDFF 

       430        440        450        460        470 
PEYMELCEPQ SYCPMHHQDH KTELLRCRSQ SKVQEGERQL REQIALLVKD MSP 

« Hide

Isoform 2 (CDC25C2) [UniParc].

Checksum: 11480DF49B3F04DD
Show »

FASTA44350,122
Isoform 3 (CDC25C3) (Sequence not available).
Isoform 4 (CDC25C4) [UniParc].

Checksum: F2DDF9DB1653BCEE
Show »

FASTA43048,851
Isoform 5 (CDC25C5) (Cdc25Cdm) [UniParc].

Checksum: 212EA5FD75672289
Show »

FASTA40045,608

References

« Hide 'large scale' references
[1]"Human homolog of fission yeast cdc25 mitotic inducer is predominantly expressed in G2."
Sadhu K., Reed B.I., Richardson H., Russell P.
Proc. Natl. Acad. Sci. U.S.A. 87:5139-5143(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CYS-70.
[2]"An additional transcript of the cdc25C gene from A431 cells encodes a functional protein."
Bureik M., Rief N., Drescher R., Jungbluth A., Montenarh M., Wagner P.
Int. J. Oncol. 17:1251-1258(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[3]NIEHS SNPs program
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]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].
[5]"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 1), VARIANT CYS-70.
Tissue: Skin.
[6]"Alternative splicing in the regulatory region of the human phosphatases CDC25A and CDC25C."
Wegener S., Hampe W., Herrmann D., Schaller H.C.
Eur. J. Cell Biol. 79:810-815(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-210 (ISOFORMS 2; 4 AND 5), VARIANT CYS-70.
[7]"Differential expression of cdc25 cell-cycle-activating phosphatases in human colorectal carcinoma."
Hernandez S., Bessa X., Bea S., Hernandez L., Nadal A., Mallofre C., Muntane J., Castells A., Fernandez P.L., Cardesa A., Campo E.
Lab. Invest. 81:465-473(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Tissue: Colon carcinoma.
[8]"Activation of p34cdc2 protein kinase by microinjection of human cdc25C into mammalian cells. Requirement for prior phosphorylation of cdc25C by p34cdc2 on sites phosphorylated at mitosis."
Strausfeld U., Fernandez A., Capony J.P., Girard F., Lautredou N., Derancourt J., Labbe J.C., Lamb N.J.
J. Biol. Chem. 269:5989-6000(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-48; THR-67; SER-122; THR-130; SER-168 AND SER-214.
[9]"The physical association and phosphorylation of Cdc25C protein phosphatase by Prk."
Ouyang B., Li W., Pan H., Meadows J., Hoffmann I., Dai W.
Oncogene 18:6029-6036(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY PLK3.
[10]"The human polo-like kinase, PLK, regulates cdc2/cyclin B through phosphorylation and activation of the cdc25C phosphatase."
Roshak A.K., Capper E.A., Imburgia C., Fornwald J., Scott G., Marshall L.A.
Cell. Signal. 12:405-411(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY PLK1.
[11]"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-216, INTERACTION WITH MAPK14 AND 14-3-3 PROTEINS.
[12]"Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates."
Elia A.E., Cantley L.C., Yaffe M.B.
Science 299:1228-1231(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLK1, MUTAGENESIS OF SER-129 AND THR-130.
[13]"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-216.
Tissue: Testis.
[14]"Cdc25C phosphorylation on serine 191 by Plk3 promotes its nuclear translocation."
Bahassi el M., Hennigan R.F., Myer D.L., Stambrook P.J.
Oncogene 23:2658-2663(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-191 AND SER-198, MUTAGENESIS OF SER-191.
[15]"The human immunodeficiency virus Vpr protein binds Cdc25C: implications for G2 arrest."
Goh W.C., Manel N., Emerman M.
Virology 318:337-349(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 VPR, MUTAGENESIS OF GLU-352 AND LYS-359.
[16]"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-216 BY MAPKAPK2.
[17]"Human Plk4 phosphorylates Cdc25C."
Bonni S., Ganuelas M.L., Petrinac S., Hudson J.W.
Cell Cycle 7:545-547(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY PLK4.
[18]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-168 AND SER-472, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; THR-48; SER-57; SER-61; SER-64 AND THR-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-64 AND THR-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M34065 mRNA. Translation: AAA35666.1.
AJ304504 mRNA. Translation: CAC19192.1.
AY497474 Genomic DNA. Translation: AAR32098.1.
CH471062 Genomic DNA. Translation: EAW62145.1.
CH471062 Genomic DNA. Translation: EAW62149.1.
BC019089 mRNA. Translation: AAH19089.1.
AF277723 mRNA. Translation: AAG41885.1.
AF277725 mRNA. Translation: AAG41887.1.
AF277726 mRNA. Translation: AAG41888.1.
AF312681 mRNA. Translation: AAL26835.1.
PIRA38874. I59168.
RefSeqNP_001274511.1. NM_001287582.1.
NP_001781.2. NM_001790.4.
NP_073720.1. NM_022809.3.
UniGeneHs.656.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BZIX-ray2.10E126-134[»]
3OP3X-ray2.63A270-462[»]
ProteinModelPortalP30307.
SMRP30307. Positions 280-448.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107430. 32 interactions.
DIPDIP-24183N.
IntActP30307. 7 interactions.
MINTMINT-86355.
STRING9606.ENSP00000321656.

Chemistry

BindingDBP30307.
ChEMBLCHEMBL2378.

PTM databases

PhosphoSiteP30307.

Polymorphism databases

DMDM116242631.

Proteomic databases

PaxDbP30307.
PRIDEP30307.

Protocols and materials databases

DNASU995.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323760; ENSP00000321656; ENSG00000158402. [P30307-1]
ENST00000348983; ENSP00000345205; ENSG00000158402. [P30307-4]
ENST00000356505; ENSP00000348898; ENSG00000158402. [P30307-2]
ENST00000357274; ENSP00000349821; ENSG00000158402. [P30307-3]
ENST00000415130; ENSP00000392631; ENSG00000158402. [P30307-4]
ENST00000513970; ENSP00000424795; ENSG00000158402. [P30307-1]
ENST00000514555; ENSP00000425470; ENSG00000158402. [P30307-2]
GeneID995.
KEGGhsa:995.
UCSCuc003lcp.1. human. [P30307-1]
uc003lcq.1. human. [P30307-4]

Organism-specific databases

CTD995.
GeneCardsGC05M137620.
HGNCHGNC:1727. CDC25C.
HPACAB003800.
MIM157680. gene.
neXtProtNX_P30307.
PharmGKBPA100.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5105.
HOVERGENHBG052501.
InParanoidP30307.
KOK05867.
OMATVSLCDI.
OrthoDBEOG7288R1.
PhylomeDBP30307.
TreeFamTF101056.

Enzyme and pathway databases

BRENDA3.1.3.48. 2681.
ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressP30307.
BgeeP30307.
CleanExHS_CDC25C.
GenevestigatorP30307.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
InterProIPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PfamPF06617. M-inducer_phosp. 2 hits.
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

ChiTaRSCDC25C. human.
EvolutionaryTraceP30307.
GeneWikiCDC25C.
GenomeRNAi995.
NextBio4178.
PROP30307.
SOURCESearch...

Entry information

Entry nameMPIP3_HUMAN
AccessionPrimary (citable) accession number: P30307
Secondary accession number(s): D3DQB8 expand/collapse secondary AC list , Q96PL3, Q9H168, Q9H2E8, Q9H2E9, Q9H2F1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 148 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 5

Human chromosome 5: entries, gene names and cross-references to MIM