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P11084 (PP4C_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length307 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 DSB repair. Dephosphorylates NDEL1 at CDK1 phosphorylation sites and negatively regulates CDK1 activity in interphase By similarity. 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.

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 2 manganese ions 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. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome.

Sequence similarities

Belongs to the PPP phosphatase family. PP-4 (PP-X) subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 307306Serine/threonine-protein phosphatase 4 catalytic subunit
PRO_0000058885

Sites

Active site1151Proton donor By similarity
Metal binding541Manganese 1 By similarity
Metal binding561Manganese 1 By similarity
Metal binding821Manganese 1 By similarity
Metal binding821Manganese 2 By similarity
Metal binding1141Manganese 2 By similarity
Metal binding1641Manganese 2 By similarity
Metal binding2381Manganese 2 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue3071Leucine methyl ester Ref.4

Sequences

Sequence LengthMass (Da)Tools
P11084 [UniParc].

Last modified August 1, 1992. Version 2.
Checksum: 364A1641F8B22B41

FASTA30735,037
        10         20         30         40         50         60 
MAEISDLDRQ IEQLLRCELI 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

[1]"Protein serine/threonine phosphatases; an expanding family."
Cohen P.T.W., Brewis N.D., Hughes V., Mann D.J.
FEBS Lett. 268:355-359(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: New Zealand white.
Tissue: Liver.
[2]"PPX, a novel protein serine/threonine phosphatase localized to centrosomes."
Brewis N.D., Street A.J., Prescott A.R., Cohen P.T.W.
EMBO J. 12:987-996(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: New Zealand white.
Tissue: Liver.
[3]"Identification of a novel protein phosphatase catalytic subunit by cDNA cloning."
da Cruz e Silva O.B., da Cruz e Silva E.F., Cohen P.T.W.
FEBS Lett. 242:106-110(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 105-307.
Strain: New Zealand white.
Tissue: Liver.
[4]"Carboxymethylation of nuclear protein serine/threonine phosphatase X."
Kloeker S., Bryant J.C., Strack S., Colbran R.J., Wadzinski B.E.
Biochem. J. 327:481-486(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LEU-307.
[5]"A novel 50 kDa protein forms complexes with protein phosphatase 4 and is located at centrosomal microtubule organizing centres."
Hastie C.J., Carnegie G.K., Morrice N., Cohen P.T.W.
Biochem. J. 347:845-855(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP4R2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14031 mRNA. Translation: CAA32191.1.
S57412 mRNA. Translation: AAB25913.1.
PIRPARBA2. S36193.
RefSeqNP_001075792.1. NM_001082323.1.
UniGeneOcu.3272.

3D structure databases

ProteinModelPortalP11084.
SMRP11084. Positions 6-307.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000005480.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009163.

Organism-specific databases

CTD5531.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172696.
HOVERGENHBG000216.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePP4C_RABIT
AccessionPrimary (citable) accession number: P11084
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: August 1, 1992
Last modified: June 11, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families