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P11084

- PP4C_RABIT

UniProt

P11084 - PP4C_RABIT

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Protein

Serine/threonine-protein phosphatase 4 catalytic subunit

Gene

PPP4C

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi54 – 541Manganese 1By similarity
Metal bindingi56 – 561Manganese 1By similarity
Metal bindingi82 – 821Manganese 1By similarity
Metal bindingi82 – 821Manganese 2By similarity
Metal bindingi114 – 1141Manganese 2By similarity
Active sitei115 – 1151Proton donorBy similarity
Metal bindingi164 – 1641Manganese 2By similarity
Metal bindingi238 – 2381Manganese 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein serine/threonine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. dephosphorylation Source: GOC
  2. regulation of double-strand break repair via homologous recombination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 4 catalytic subunit (EC:3.1.3.16)
Short name:
PP4C
Short name:
Pp4
Alternative name(s):
Protein phosphatase X
Short name:
PP-X
Gene namesi
Name:PPP4C
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-KW
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 307306Serine/threonine-protein phosphatase 4 catalytic subunitPRO_0000058885Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei307 – 3071Leucine methyl ester1 Publication

Keywords - PTMi

Acetylation, Methylation

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000005480.

Structurei

3D structure databases

ProteinModelPortaliP11084.
SMRiP11084. Positions 6-307.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172696.
HOVERGENiHBG000216.
InParanoidiP11084.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11084-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEISDLDRQ IEQLLRCELI KESEVKALCA KAREILVEES NVQRVDSPVT
60 70 80 90 100
VCGDIHGQFY DLKELFRVGG DVPETNYLFM GDFVDRGFYS VETFLLLLAL
110 120 130 140 150
KVRYPDRITL IRGNHESRQI TQVYGFYDEC LRKYGSVTVW RYCTEIFDYL
160 170 180 190 200
SLSAIIDGKI FCVHGGLSPS IQTLDQIRTI DRKQEVPHDG PMCDLLWSDP
210 220 230 240 250
EDTTGWGVSP RGAGYLFGSD VVAQFNAAND IDMICRAHQL VMEGYKWHFN
260 270 280 290 300
ETVLTVWSAP NYCYRCGNVA AILELDEHLQ KDFIIFEAAP QETRGIPSKK

PVADYFL
Length:307
Mass (Da):35,037
Last modified:August 1, 1992 - v2
Checksum:i364A1641F8B22B41
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14031 mRNA. Translation: CAA32191.1.
S57412 mRNA. Translation: AAB25913.1.
PIRiS36193. PARBA2.
RefSeqiNP_001075792.1. NM_001082323.1.
UniGeneiOcu.3272.

Genome annotation databases

GeneIDi100009163.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14031 mRNA. Translation: CAA32191.1 .
S57412 mRNA. Translation: AAB25913.1 .
PIRi S36193. PARBA2.
RefSeqi NP_001075792.1. NM_001082323.1.
UniGenei Ocu.3272.

3D structure databases

ProteinModelPortali P11084.
SMRi P11084. Positions 6-307.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000005480.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100009163.

Organism-specific databases

CTDi 5531.

Phylogenomic databases

eggNOGi COG0639.
HOGENOMi HOG000172696.
HOVERGENi HBG000216.
InParanoidi P11084.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiPP4C_RABIT
AccessioniPrimary (citable) accession number: P11084
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: August 1, 1992
Last modified: November 26, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3