Serine/threonine-protein phosphatase 4 catalytic subunit

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P97470 (PP4C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 111. History...

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

Documents (2) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase 4 catalytic subunit
Short name=PP4C
Short name=Pp4
EC=3.1.3.16

Alternative name(s):
Protein phosphatase X
Short name=PP-X

Gene names

Name:	Ppp4c
Synonyms:	Ppp4, Ppx

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	307 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein phosphatase that is involved in many processes such as microtubule organization at centrosomes, maturation of spliceosomal snRNPs, apoptosis, DNA repair, tumor necrosis factor (TNF)-alpha signaling, activation of c-Jun N-terminal kinase MAPK8, regulation of histone acetylation, DNA damage checkpoint signaling, NF-kappa-B activation and cell migration. The PPP4C-PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on Ser-140 (gamma-H2AFX) generated during DNA replication and required for DNA double strand break repair By similarity. Dephosphorylates NDEL1 at CDK1 phosphorylation sites and negatively regulates CDK1 activity in interphase. In response to DNA damage, catalyzes RPA2 dephosphorylation, an essential step for DNA repair since it allows the efficient RPA2-mediated recruitment of RAD51 to chromatin By similarity. Ref.6
Catalytic activity	A phosphoprotein + H₂O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity.
Subunit structure	Serine/threonine-protein phosphatase 4 (PP4) occurs in different assemblies of the catalytic and one or more regulatory subunits. Component of the PP4 complexes PPP4C-PPP4R1, PPP4C-PPP4R2, PPP4C-PPP4R2-PPP4R3A, PPP4C-PPP4R2-PPP4R3B and PPP4C-PPP4R4. The PPP4C-PPP4R2 complex appears to be a tetramer composed of 2 molecules of PPP4C and 2 molecules of PPP4R2. Interacts with REL, NFKB1/p50 and RELA. Interacts with SMN1 AND GEMIN4. Interacts with IRS4 (phosphorylated). Interacts with SMEK1/PPP4R3A; the interaction requires PP4R2. Interacts with HDAC3 By similarity. Ref.5
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › cytoskeleton › centrosome.
Sequence similarities	Belongs to the PPP phosphatase family. PP-4 (PP-X) subfamily.
Sequence caution	The sequence AAB38494.1 differs from that shown. Reason: Frameshift at positions 101 and 106.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Nucleus
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Methylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	microtubule cytoskeleton organization Non-traceable author statement. Source: UniProtKB regulation of double-strand break repair via homologous recombination Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	centrosome Non-traceable author statement. Source: UniProtKB cytoplasm Inferred from direct assay PubMed 20876121. Source: MGI nucleus Non-traceable author statement. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: Compara protein phosphatase 4 complex Inferred from direct assay PubMed 20876121. Source: MGI
Molecular_function	NF-kappaB-inducing kinase activity Non-traceable author statement Ref.1. Source: UniProtKB metal ion binding Non-traceable author statement. Source: UniProtKB protein serine/threonine phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 307

306

Serine/threonine-protein phosphatase 4 catalytic subunit

PRO_0000058884

Sites

Active site

115

Proton donor By similarity

Metal binding

Iron By similarity

Metal binding

Iron By similarity

Metal binding

Iron By similarity

Metal binding

Manganese By similarity

Metal binding

114

Manganese By similarity

Metal binding

164

Manganese By similarity

Metal binding

238

Manganese By similarity

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

307

Leucine methyl ester By similarity

Experimental info

Sequence conflict

95 – 96

LL → FF in AAB38494. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P97470 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: D6FE470A5C6CBCAC
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FASTA

307

35,080

        10         20         30         40         50         60 
MAEISDLDRQ IEQLRRCELI KESEVKALCA KAREILVEES NVQRVDSPVT VCGDIHGQFY 

        70         80         90        100        110        120 
DLKELFRVGG DVPETNYLFM GDFVDRGFYS VETFLLLLAL KVRYPDRITL IRGNHESRQI 

       130        140        150        160        170        180 
TQVYGFYDEC LRKYGSVTVW RYCTEIFDYL SLSAIIDGKI FCVHGGLSPS IQTLDQIRTI 

       190        200        210        220        230        240 
DRKQEVPHDG PMCDLLWSDP EDTTGWGVSP RGAGYLFGSD VVAQFNAAND IDMICRAHQL 

       250        260        270        280        290        300 
VMEGYKWHFN ETVLTVWSAP NYCYRCGNVA AILELDEHLQ KDFIIFEAAP QETRGIPSKK 


PVADYFL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Protein phosphatase X interacts with c-Rel and stimulates c-Rel/nuclear factor kappaB activity." Hu M.C.-T., Tang-Oxley Q., Qiu W.R., Wang Y.-P., Mihindukulasuriya K.A., Afshar R., Tan T.-H. J. Biol. Chem. 273:33561-33565(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genomic structure of the mouse PP4 gene: a developmentally regulated protein phosphatase." Hu M.C.-T., Shui J.W., Mihindukulasuriya K.A., Tan T.-H. Gene 278:89-99(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/SvJ.
[3]	"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: Mammary tumor.
[4]	Sussman D.J. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 79-293. Strain: BALB/c.
[5]	"PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4." Chen G.I., Tisayakorn S., Jorgensen C., D'Ambrosio L.M., Goudreault M., Gingras A.-C. J. Biol. Chem. 283:29273-29284(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPP4C.
[6]	"Protein phosphatase 4 catalytic subunit regulates Cdk1 activity and microtubule organization via NDEL1 dephosphorylation." Toyo-oka K., Mori D., Yano Y., Shiota M., Iwao H., Goto H., Inagaki M., Hiraiwa N., Muramatsu M., Wynshaw-Boris A., Yoshiki A., Hirotsune S. J. Cell Biol. 180:1133-1147(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF088911 mRNA. Translation: AAC96297.1. AF378669 Genomic DNA. Translation: AAL35110.1. BC001993 mRNA. Translation: AAH01993.1. U79747 mRNA. Translation: AAB38494.1. Frameshift.
IPI	IPI00109415.
RefSeq	NP_062648.1. NM_019674.3.
UniGene	Mm.41998.
3D structure databases
ProteinModelPortal	P97470.
ModBase	Search...
Protein-protein interaction databases
IntAct	P97470. 1 interaction.
STRING	10090.ENSMUSP00000032936.
PTM databases
PhosphoSite	P97470.
Proteomic databases
PaxDb	P97470.
PRIDE	P97470.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000032936; ENSMUSP00000032936; ENSMUSG00000030697.
GeneID	56420.
KEGG	mmu:56420.
Organism-specific databases
CTD	5531.
MGI	MGI:1891763. Ppp4c.
Phylogenomic databases
eggNOG	COG0639.
HOGENOM	HOG000172696.
HOVERGEN	HBG000216.
InParanoid	P97470.
KO	K15423.
OMA	GFKWHFN.
OrthoDB	EOG4NS3BV.
Gene expression databases
ArrayExpress	P97470.
Bgee	P97470.
CleanEx	MM_PPP4C.
Genevestigator	P97470.
GermOnline	ENSMUSG00000030697. Mus musculus.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PPP4C. mouse.
NextBio	21426.
SOURCE	Search...

Entry information

Entry name

PP4C_MOUSE

Accession

Primary (citable) accession number: P97470
Secondary accession number(s): P33172

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	March 1, 2004
Last modified:	May 1, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

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