Protein phosphatase 1D - Homo sapiens (Human)

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O15297 (PPM1D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 119. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein phosphatase 1D
EC=3.1.3.16

Alternative name(s):
Protein phosphatase 2C isoform delta
Short name=PP2C-delta
Protein phosphatase magnesium-dependent 1 delta
p53-induced protein phosphatase 1

Gene names

Name:	PPM1D
Synonyms:	WIP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	605 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for the relief of p53-dependent checkpoint mediated cell cycle arrest. Binds to and dephosphorylates 'Ser-15' of TP53 and 'Ser-345' of CHEK1 which contributes to the functional inactivation of these proteins. Ref.5 Ref.6
Catalytic activity	A phosphoprotein + H₂O = a protein + phosphate.
Cofactor	Binds 2 magnesium or manganese ions per subunit By similarity.
Subunit structure	Interacts with CHEK1 and CHEK2; dephosphorylates them. Ref.5 Ref.6
Induction	By p53/TP53. Ref.1 Ref.5
Sequence similarities	Belongs to the PP2C family. Contains 1 PP2C-like domain.

Ontologies

Keywords
Biological process	Cell cycle
Ligand	Magnesium Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Traceable author statement Ref.1. Source: ProtInc peptidyl-threonine dephosphorylation Inferred from direct assay PubMed 20801214. Source: UniProtKB response to bacterium Inferred from electronic annotation. Source: Compara response to radiation Traceable author statement Ref.1. Source: ProtInc
Cellular_component	nucleus Traceable author statement Ref.1. Source: ProtInc
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine phosphatase activity Inferred from direct assay PubMed 20801214. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MDM2	Q00987	4	EBI-1551512,EBI-389668

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 605

605

Protein phosphatase 1D

PRO_0000057752

Regions

Domain

61 – 378

318

PP2C-like

Region

1 – 101

101

Interaction with CHEK1

Sites

Metal binding

105

Manganese 1 By similarity

Metal binding

105

Manganese 2 By similarity

Metal binding

106

Manganese 1; via carbonyl oxygen By similarity

Metal binding

314

Manganese 2 By similarity

Metal binding

366

Manganese 2 By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.7

Experimental info

Mutagenesis

314

D → A: Abrogates phosphatase activity. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

O15297 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: E6C5884CF04008B7
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FASTA

605

66,675

        10         20         30         40         50         60 
MAGLYSLGVS VFSDQGGRKY MEDVTQIVVE PEPTAEEKPS PRRSLSQPLP PRPSPAALPG 

        70         80         90        100        110        120 
GEVSGKGPAV AAREARDPLP DAGASPAPSR CCRRRSSVAF FAVCDGHGGR EAAQFAREHL 

       130        140        150        160        170        180 
WGFIKKQKGF TSSEPAKVCA AIRKGFLACH LAMWKKLAEW PKTMTGLPST SGTTASVVII 

       190        200        210        220        230        240 
RGMKMYVAHV GDSGVVLGIQ DDPKDDFVRA VEVTQDHKPE LPKERERIEG LGGSVMNKSG 

       250        260        270        280        290        300 
VNRVVWKRPR LTHNGPVRRS TVIDQIPFLA VARALGDLWS YDFFSGEFVV SPEPDTSVHT 

       310        320        330        340        350        360 
LDPQKHKYII LGSDGLWNMI PPQDAISMCQ DQEEKKYLMG EHGQSCAKML VNRALGRWRQ 

       370        380        390        400        410        420 
RMLRADNTSA IVICISPEVD NQGNFTNEDE LYLNLTDSPS YNSQETCVMT PSPCSTPPVK 

       430        440        450        460        470        480 
SLEEDPWPRV NSKDHIPALV RSNAFSENFL EVSAEIAREN VQGVVIPSKD PEPLEENCAK 

       490        500        510        520        530        540 
ALTLRIHDSL NNSLPIGLVP TNSTNTVMDQ KNLKMSTPGQ MKAQEIERTP PTNFKRTLEE 

       550        560        570        580        590        600 
SNSGPLMKKH RRNGLSRSSG AQPASLPTTS QRKNSVKLTM RRRLRGQKKI GNPLLHQHRK 


TVCVC

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Wip1, a novel human protein phosphatase that is induced in response to ionizing radiation in a p53-dependent manner." Fiscella M., Zhang H., Fan S., Sakaguchi K., Shen S., Mercer W.E., Vande Woude G.F., O'Connor P.M., Appella E. Proc. Natl. Acad. Sci. U.S.A. 94:6048-6053(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	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. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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]. Tissue: Skin.
[5]	"PPM1D dephosphorylates Chk1 and p53 and abrogates cell cycle checkpoints." Lu X., Nannenga B., Donehower L.A. Genes Dev. 19:1162-1174(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CHEK1, INDUCTION, MUTAGENESIS OF ASP-314.
[6]	"Regulation of the antioncogenic Chk2 kinase by the oncogenic Wip1 phosphatase." Fujimoto H., Onishi N., Kato N., Takekawa M., Xu X.Z., Kosugi A., Kondo T., Imamura M., Oishi I., Yoda A., Minami Y. Cell Death Differ. 13:1170-1180(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN APOPTOSIS, FUNCTION IN DEPHOSPHORYLATION OF CHEK2, INTERACTION WITH CHEK2.
[7]	"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-40, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	U78305 mRNA. Translation: AAB61637.1. BT009780 mRNA. Translation: AAP88782.1. CH471179 Genomic DNA. Translation: EAW51408.1. BC016480 mRNA. Translation: AAH16480.1.
IPI	IPI00005782.
RefSeq	NP_003611.1. NM_003620.3.
UniGene	Hs.286073.
3D structure databases
ProteinModelPortal	O15297.
ModBase	Search...
Protein-protein interaction databases
IntAct	O15297. 1 interaction.
STRING	9606.ENSP00000306682.
PTM databases
PhosphoSite	O15297.
Proteomic databases
PaxDb	O15297.
PRIDE	O15297.
Protocols and materials databases
DNASU	8493.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000305921; ENSP00000306682; ENSG00000170836.
GeneID	8493.
KEGG	hsa:8493.
UCSC	uc002iyt.2. human.
Organism-specific databases
CTD	8493.
GeneCards	GC17P058677.
HGNC	HGNC:9277. PPM1D.
HPA	CAB009474. HPA022277.
MIM	605100. gene.
neXtProt	NX_O15297.
PharmGKB	PA33605.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0631.
HOGENOM	HOG000231949.
HOVERGEN	HBG058897.
InParanoid	O15297.
KO	K10147.
OMA	NAFSENF.
OrthoDB	EOG41JZCG.
PhylomeDB	O15297.
Gene expression databases
ArrayExpress	O15297.
Bgee	O15297.
CleanEx	HS_PPM1D.
Genevestigator	O15297.
Family and domain databases
Gene3D	3.60.40.10. 2 hits.
InterPro	IPR001932. PP2C-like. IPR000222. PP2C_Mn2_Asp60_BS. IPR015655. Protein_Pase_2C. [Graphical view]
PANTHER	PTHR13832. PTHR13832. 1 hit.
Pfam	PF00481. PP2C. 1 hit. [Graphical view]
SMART	SM00332. PP2Cc. 1 hit. [Graphical view]
SUPFAM	SSF81606. PP2C-related. 1 hit.
PROSITE	PS01032. PP2C. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	O15297.
ChEMBL	CHEMBL1938224.
GenomeRNAi	8493.
NextBio	31775.
SOURCE	Search...

Entry information

Entry name

PPM1D_HUMAN

Accession

Primary (citable) accession number: O15297
Secondary accession number(s): Q53XP4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 119 of the entry and version 1 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.

Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents