P30304 (MPIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
M-phase inducer phosphatase 1
EC=3.1.3.48

Alternative name(s):
Dual specificity phosphatase Cdc25A

Gene names

Name:

CDC25A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	524 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. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Enzyme regulation	Stimulated by B-type cyclins. Stimulated by PIM1-mediated phosphorylation.
Subunit structure	Interacts with CCNB1/cyclin B1. Interacts with YWHAE/14-3-3 epsilon when phosphorylated. Interacts with CUL1 specifically when CUL1 is neddylated and active. Interacts with BTRC/BTRCP1 and FBXW11/BTRCP2. Interactions with CUL1, BTRC and FBXW11 are enhanced upon DNA damage. Interacts with PIM1. Interacts with CHEK2; mediates CDC25A phosphorylation and degradation in response to infrared-induced DNA damages. Ref.6 Ref.10 Ref.13 Ref.14
Domain	The phosphodegron motif mediates interaction with specific F-box proteins when phosphorylated. Putative phosphorylation sites at Ser-79 and Ser-82 appear to be essential for this interaction. Ref.7
Post-translational modification	Phosphorylated by CHEK1 on Ser-76, Ser-124, Ser-178, Ser-279, Ser-293 and Thr-507 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-124, Ser-279, and Ser-293 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-178 and Thr-507 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-76, Ser-124, Ser-178, Ser-279 and Ser-293 may also promote ubiquitin-dependent proteolysis of CDC25A by the SCF complex. Phosphorylation of CDC25A at Ser-76 by CHEK1 primes it for subsequent phosphorylation at Ser-79, Ser-82 and Ser-88 by NEK11. Phosphorylation by NEK11 is required for BTRC-mediated polyubiquitination and degradation. Phosphorylation by PIM1 leads to an increase in phosphatase activity. Phosphorylated by PLK3 following DNA damage, leading to promote its ubiquitination and degradation. Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.18 Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex that contains FZR1/CDH1 during G1 phase leading to its degradation by the proteasome. Ubiquitinated by a SCF complex containing BTRC and FBXW11 during S phase leading to its degradation by the proteasome. Deubiquitination by USP17L2/DUB3 leads to its stabilization. Ref.7 Ref.10 Ref.17 Ref.18
Sequence similarities	Belongs to the MPI phosphatase family. Contains 1 rhodanese domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Traceable author statement. Source: Reactome G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome cell cycle checkpoint Traceable author statement. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Traceable author statement Ref.5. Source: UniProtKB cellular response to UV Inferred from direct assay PubMed 19966869. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC regulation of cyclin-dependent protein serine/threonine kinase activity Traceable author statement Ref.5. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RAF1	P04049	4	EBI-747671,EBI-365996
YWHAB	P31946	8	EBI-747671,EBI-359815

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P30304-1)

Also known as: CDC25A1;

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: P30304-2)

Also known as: CDC25A2;

The sequence of this isoform differs from the canonical sequence as follows:
     144-183: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 524

524

M-phase inducer phosphatase 1

PRO_0000198641

Regions

Domain

376 – 482

107

Rhodanese

Motif

74 – 84

11

Phosphodegron

Motif

141 – 143

3

KEN box

Sites

Active site

431

1

Amino acid modifications

Modified residue

76

1

Phosphoserine; by CHEK1 Ref.10 Ref.12

Modified residue

79

1

Phosphoserine; by NEK11 Ref.15

Modified residue

82

1

Phosphoserine; by NEK11 Ref.15 Ref.16

Modified residue

88

1

Phosphoserine; by NEK11 Ref.15 Ref.16

Modified residue

124

1

Phosphoserine; by CHEK1 and CHEK2 Ref.6 Ref.8 Ref.9 Ref.10 Ref.12

Modified residue

178

1

Phosphoserine; by CHEK1 Ref.9 Ref.12 Ref.13

Modified residue

279

1

Phosphoserine; by CHEK1 and CHEK2 Ref.9

Modified residue

293

1

Phosphoserine; by CHEK1 and CHEK2 Ref.9

Modified residue

507

1

Phosphothreonine; by CHEK1 Ref.13

Modified residue

513

1

Phosphoserine; by PLK3 Ref.18

Modified residue

519

1

Phosphoserine; by PLK3 Ref.18

Natural variations

Alternative sequence

144 – 183

40

Missing in isoform 2.

VSP_000860

Natural variant

88

1

S → F. Ref.3
Corresponds to variant rs3731499 [ dbSNP | Ensembl ].

VAR_020932

Natural variant

182

1

R → G. Ref.1
Corresponds to variant rs6771386 [ dbSNP | Ensembl ].

VAR_023532

Natural variant

182

1

R → W.
Corresponds to variant rs6771386 [ dbSNP | Ensembl ].

VAR_023533

Experimental info

Mutagenesis

76

1

S → A: Abolishes ubiquitination and impairs CHEK1-dependent degradation following checkpoint activation. Ref.10 Ref.12

Mutagenesis

79

1

S → A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. Ref.10

Mutagenesis

81

1

D → A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. Ref.10

Mutagenesis

82

1

S → A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. Ref.10

Mutagenesis

124

1

S → A: Abrogates phosphorylation by CHEK2 and infrared-induced degradation. Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-178; A-279 and A-293. Ref.6 Ref.8 Ref.9 Ref.12

Mutagenesis

141 – 143

3

KEN → AAA: Prevents ubiquitination and subsequent degradation by the APC/C ubiquitin ligase complex. Ref.7

Mutagenesis

178

1

S → A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-279 and A-293. Abrogates 14-3-3 protein binding. Ref.9 Ref.12 Ref.13

Mutagenesis

279

1

S → A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-293. Ref.9

Mutagenesis

293

1

S → A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-279. Ref.9

Mutagenesis

431

1

C → S: Abolishes phosphatase activity. Ref.11 Ref.13

Mutagenesis

507

1

T → A: Abrogates 14-3-3 protein binding; increases binding to cyclin B1. Ref.13

Mutagenesis

513

1

S → A: Increased stability following IR treatment. Ref.18

Mutagenesis

513

1

S → D: Mimicks phosphorylation state, leading to promote degradation following IR treatment. Ref.18

Mutagenesis

514

1

K → L: Abrogates binding to CCNB1; when associated with L-520. Ref.13

Mutagenesis

519

1

S → A: Increased stability following IR treatment. Ref.18

Mutagenesis

519

1

S → D: Mimicks phosphorylation state, leading to promote degradation following IR treatment. Ref.18

Mutagenesis

520

1

R → L: Abrogates binding to CCNB1; when associated with L-514. Ref.13

Sequence conflict

6 – 10

5

EPPHR → SPAP in AAA58415. Ref.1

Sequence conflict

180 – 181

2

PA → QL in AAA58415. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

524

Helix Strand Turn

Details...

Beta strand

341 – 344

4

Helix

362 – 369

8

Turn

370 – 376

7

Beta strand

377 – 384

8

Helix

388 – 392

5

Helix

405 – 411

7

Turn

412 – 414

3

Beta strand

423 – 430

8

Beta strand

432 – 436

5

Helix

437 – 451

15

Beta strand

463 – 466

4

Helix

469 – 477

9

Helix

478 – 480

3

Beta strand

481 – 484

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (CDC25A1) [UniParc]. Last modified July 19, 2004. Version 2. Checksum: B2F6B792D4E6122B	FASTA	524	59,087
	10 20 30 40 50 60 MELGPEPPHR RRLLFACSPP PASQPVVKAL FGASAAGGLS PVTNLTVTMD QLQGLGSDYE 70 80 90 100 110 120 QPLEVKNNSN LQRMGSSEST DSGFCLDSPG PLDSKENLEN PMRRIHSLPQ KLLGCSPALK 130 140 150 160 170 180 RSHSDSLDHD IFQLIDPDEN KENEAFEFKK PVRPVSRGCL HSHGLQEGKD LFTQRQNSAP 190 200 210 220 230 240 ARMLSSNERD SSEPGNFIPL FTPQSPVTAT LSDEDDGFVD LLDGENLKNE EETPSCMASL 250 260 270 280 290 300 WTAPLVMRTT NLDNRCKLFD SPSLCSSSTR SVLKRPERSQ EESPPGSTKR RKSMSGASPK 310 320 330 340 350 360 ESTNPEKAHE TLHQSLSLAS SPKGTIENIL DNDPRDLIGD FSKGYLFHTV AGKHQDLKYI 370 380 390 400 410 420 SPEIMASVLN GKFANLIKEF VIIDCRYPYE YEGGHIKGAV NLHMEEEVED FLLKKPIVPT 430 440 450 460 470 480 DGKRVIVVFH CEFSSERGPR MCRYVRERDR LGNEYPKLHY PELYVLKGGY KEFFMKCQSY 490 500 510 520 CEPPSYRPMH HEDFKEDLKK FRTKSRTWAG EKSKREMYSR LKKL
	Isoform 2 (CDC25A2) [UniParc]. Checksum: AE6326F34B704D4B	FASTA	484	54,551
	10 20 30 40 50 60 MELGPEPPHR RRLLFACSPP PASQPVVKAL FGASAAGGLS PVTNLTVTMD QLQGLGSDYE 70 80 90 100 110 120 QPLEVKNNSN LQRMGSSEST DSGFCLDSPG PLDSKENLEN PMRRIHSLPQ KLLGCSPALK 130 140 150 160 170 180 RSHSDSLDHD IFQLIDPDEN KENLSSNERD SSEPGNFIPL FTPQSPVTAT LSDEDDGFVD 190 200 210 220 230 240 LLDGENLKNE EETPSCMASL WTAPLVMRTT NLDNRCKLFD SPSLCSSSTR SVLKRPERSQ 250 260 270 280 290 300 EESPPGSTKR RKSMSGASPK ESTNPEKAHE TLHQSLSLAS SPKGTIENIL DNDPRDLIGD 310 320 330 340 350 360 FSKGYLFHTV AGKHQDLKYI SPEIMASVLN GKFANLIKEF VIIDCRYPYE YEGGHIKGAV 370 380 390 400 410 420 NLHMEEEVED FLLKKPIVPT DGKRVIVVFH CEFSSERGPR MCRYVRERDR LGNEYPKLHY 430 440 450 460 470 480 PELYVLKGGY KEFFMKCQSY CEPPSYRPMH HEDFKEDLKK FRTKSRTWAG EKSKREMYSR LKKL

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-182.
[2]	Varmeh-Ziaie S., Manfredi J.J. Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]	NIEHS SNPs program Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-88.
[4]	"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). Tissue: Lymph.
[5]	"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 37-234 (ISOFORM 2).
[6]	"The ATM-Chk2-Cdc25A checkpoint pathway guards against radioresistant DNA synthesis." Falck J., Mailand N., Syljuaasen R.G., Bartek J., Lukas J. Nature 410:842-847(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHEK2, PHOSPHORYLATION AT SER-124 BY CHEK2, MUTAGENESIS OF SER-124.
[7]	"Dual mode of degradation of Cdc25 A phosphatase." Donzelli M., Squatrito M., Ganoth D., Hershko A., Pagano M., Draetta G.F. EMBO J. 21:4875-4884(2002) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION BY THE APC/C UBIQUITIN LIGASE COMPLEX, DOMAIN KEN BOX MOTIF, MUTAGENESIS OF 141-LYS--ASN-143.
[8]	"Disruption of the checkpoint kinase 1/cell division cycle 25A pathway abrogates ionizing radiation-induced S and G2 checkpoints." Zhao H., Watkins J.L., Piwnica-Worms H. Proc. Natl. Acad. Sci. U.S.A. 99:14795-14800(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-124, MUTAGENESIS OF SER-124.
[9]	"Chk1 regulates the S phase checkpoint by coupling the physiological turnover and ionizing radiation-induced accelerated proteolysis of Cdc25A." Soerensen C.S., Syljuaesen R.G., Falck J., Schroeder T., Roennstrand L., Khanna K.K., Zhou B.-B., Bartek J., Lukas J. Cancer Cell 3:247-258(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-124; SER-178; SER-279 AND SER-293, MUTAGENESIS OF SER-124; SER-178; SER-279 AND SER-293.
[10]	"SCFbeta-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase." Jin J., Shirogane T., Xu L., Nalepa G., Qin J., Elledge S.J., Harper J.W. Genes Dev. 17:3062-3074(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BTRC; CUL1 AND FBXW11, PHOSPHODEGRON MOTIF, PHOSPHORYLATION AT SER-76 AND SER-124, UBIQUITINATION, MUTAGENESIS OF SER-76; SER-79; ASP-81 AND SER-82.
[11]	"Chk1 mediates S and G2 arrests through Cdc25A degradation in response to DNA-damaging agents." Xiao Z., Chen Z., Gunasekera A.H., Sowin T.J., Rosenberg S.H., Fesik S., Zhang H. J. Biol. Chem. 278:21767-21773(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, MUTAGENESIS OF CYS-431.
[12]	"Phosphorylation at serine 75 is required for UV-mediated degradation of human Cdc25A phosphatase at the S-phase checkpoint." Hassepass I., Voit R., Hoffmann I. J. Biol. Chem. 278:29824-29829(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-76; SER-124 AND SER-178, MUTAGENESIS OF SER-76; SER-124 AND SER-178.
[13]	"Chk1 kinase negatively regulates mitotic function of Cdc25A phosphatase through 14-3-3 binding." Chen M.-S., Ryan C.E., Piwnica-Worms H. Mol. Cell. Biol. 23:7488-7497(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CCNB1 AND YWHAE, PHOSPHORYLATION AT SER-178 AND THR-507, MUTAGENESIS OF SER-178; CYS-431; THR-507; LYS-514 AND ARG-520.
[14]	"The oncogenic serine/threonine kinase Pim-1 directly phosphorylates and activates the G2/M specific phosphatase Cdc25C." Bachmann M., Kosan C., Xing P.X., Montenarh M., Hoffmann I., Moroy T. Int. J. Biochem. Cell Biol. 38:430-443(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PIM1.
[15]	"NEK11 regulates CDC25A degradation and the IR-induced G2/M checkpoint." Melixetian M., Klein D.K., Soerensen C.S., Helin K. Nat. Cell Biol. 11:1247-1253(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-79; SER-82 AND SER-88.
[16]	"NEK11: linking CHK1 and CDC25A in DNA damage checkpoint signaling." Soerensen C.S., Melixetian M., Klein D.K., Helin K. Cell Cycle 9:450-455(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-82 AND SER-88.
[17]	"Ubiquitin hydrolase Dub3 promotes oncogenic transformation by stabilizing Cdc25A." Pereg Y., Liu B.Y., O'Rourke K.M., Sagolla M., Dey A., Komuves L., French D.M., Dixit V.M. Nat. Cell Biol. 12:400-406(2010) [PubMed] [Europe PMC] [Abstract] Cited for: DEUBIQUITINATION BY USP17L2.
[18]	"Absence of polo-like kinase 3 in mice stabilizes Cdc25A after DNA damage but is not sufficient to produce tumors." Myer D.L., Robbins S.B., Yin M., Boivin G.P., Liu Y., Greis K.D., Bahassi el M., Stambrook P.J. Mutat. Res. 714:1-10(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-513 AND SER-519 BY PLK3, UBIQUITINATION, MUTAGENESIS OF SER-513 AND SER-519.
[19]	"Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A." Fauman E.B., Cogswell J.P., Lovejoy B., Rocque W.J., Holmes W., Montana V.G., Piwnica-Worms H., Rink M.J., Saper M.A. Cell 93:617-625(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 336-496.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M81933 mRNA. Translation: AAA58415.1.
AY137580 mRNA. Translation: AAN11305.1.
AF527417 Genomic DNA. Translation: AAM77917.1.
BC007401 mRNA. Translation: AAH07401.1.
BC018642 mRNA. Translation: AAH18642.1.
AF277722 mRNA. Translation: AAG41884.1.

IPI

IPI00216430.
IPI00220981.

PIR

A41648.

RefSeq

NP_001780.2. NM_001789.2.
NP_963861.1. NM_201567.1.

UniGene

Hs.437705.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C25	X-ray	2.30	A	337-496	[»]

ProteinModelPortal

P30304.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-166N.

IntAct

P30304. 28 interactions.

MINT

MINT-124723.

STRING

9606.ENSP00000303706.

PTM databases

PhosphoSite

P30304.

Polymorphism databases

DMDM

50403734.

Proteomic databases

PaxDb

P30304.

PRIDE

P30304.

Protocols and materials databases

DNASU

993.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000302506; ENSP00000303706; ENSG00000164045.
ENST00000351231; ENSP00000343166; ENSG00000164045.

GeneID

993.

KEGG

hsa:993.

UCSC

uc003csh.1. human.
uc003csi.1. human.

Organism-specific databases

CTD

993.

GeneCards

GC03M048173.

HGNC

HGNC:1725. CDC25A.

HPA

HPA005855.

MIM

116947. gene.

neXtProt

NX_P30304.

PharmGKB

PA26259.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5105.

HOGENOM

HOG000082672.

HOVERGEN

HBG052501.

InParanoid

P30304.

KO

K06645.

OMA

MLSSNER.

OrthoDB

EOG49P9Z6.

PhylomeDB

P30304.

Enzyme and pathway databases

BRENDA

3.1.3.48. 2681.

Reactome

REACT_115566. Cell Cycle.

Gene expression databases

ArrayExpress

P30304.

Bgee

P30304.

CleanEx

HS_CDC25A.

Genevestigator

P30304.

GermOnline

ENSG00000164045. Homo sapiens.

Family and domain databases

Gene3D

3.40.250.10. 1 hit.

InterPro

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

PANTHER

PTHR10828. PTHR10828. 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

BindingDB

P30304.

ChEMBL

CHEMBL3775.

EvolutionaryTrace

P30304.

GenomeRNAi

993.

NextBio

4164.

SOURCE

Search...

Entry information

Entry name

MPIP1_HUMAN

Accession

Primary (citable) accession number: P30304
Secondary accession number(s): Q8IZH5, Q96IL3, Q9H2F2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 129 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.