Q68FH0 · PKP4_MOUSE

  • Protein
    Plakophilin-4
  • Gene
    Pkp4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Plays a role as a regulator of Rho activity during cytokinesis. May play a role in junctional plaques (By similarity).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentadherens junction
Cellular Componentcell-cell contact zone
Cellular Componentcell-cell junction
Cellular Componentcytoplasm
Cellular Componentcytoplasmic side of plasma membrane
Cellular Componentcytoskeleton
Cellular Componentdesmosome
Cellular Componentmidbody
Cellular Componentmitotic spindle
Cellular Componentnucleus
Cellular Componentperinuclear region of cytoplasm
Cellular Componentplasma membrane
Cellular Componentpostsynaptic density
Cellular Componentspindle midzone
Cellular Componentspindle pole
Molecular Functioncadherin binding
Biological Processcell-cell adhesion
Biological Processcell-cell junction assembly
Biological Processpositive regulation of cytokinesis
Biological Processpositive regulation of GTPase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Plakophilin-4
  • Alternative names
    • Armadillo-related protein

Gene names

    • Name
      Pkp4
    • Synonyms
      Armrp

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • Czech II
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q68FH0
  • Secondary accessions
    • A2AS46
    • Q640N0
    • Q68G56
    • Q8BK47
    • Q8BVH1
    • Q9CRE3

Proteomes

Organism-specific databases

Subcellular Location

Midbody
Cell membrane
; Peripheral membrane protein
Note: Associated with the pericentrosomal region in interphase and with spindle poles during mitosis. In anaphase, during chromosome segregation, is recruited to the central microtubule bundle, focussed at the spindle midzone and ultimately localizes to the midbody at cytokinesis. Constituent of the midbody cytoskeletal matrix. Colocalized with desmoplakin at desmosomal junctional plaques in cultured epithelial cells (By similarity).

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000642901-1190Plakophilin-4
Modified residue75Phosphoserine
Modified residue84Phosphothreonine
Modified residue106Phosphoserine
Modified residue132Phosphoserine
Modified residue136Phosphoserine
Modified residue139Phosphoserine
Modified residue220Phosphoserine
Modified residue230Phosphoserine
Modified residue235Phosphoserine
Modified residue253Omega-N-methylarginine
Modified residue269Omega-N-methylarginine
Modified residue272Phosphoserine
Modified residue280Phosphoserine
Modified residue313Phosphoserine
Modified residue326Phosphoserine
Modified residue336Phosphoserine
Modified residue371Phosphotyrosine
Modified residue391Phosphoserine
Modified residue402Phosphoserine
Modified residue405Phosphoserine
Modified residue411Phosphothreonine
Modified residue414Phosphotyrosine
Modified residue421Phosphoserine
Modified residue426Phosphoserine
Modified residue437Phosphoserine
Modified residue477Phosphotyrosine
Modified residue509Phosphoserine
Modified residue511Phosphoserine
Modified residue514Phosphoserine
Modified residue775Phosphoserine
Modified residue1012Phosphothreonine
Modified residue1016Phosphothreonine
Modified residue1044Phosphoserine
Modified residue1090Phosphoserine
Modified residue1099Phosphoserine
Modified residue1133Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts (via the C-terminus) with FRMPD2 (via the PDZ 2 domain). Interacts with PDZD2. Interacts with RHOA; the interaction is detected at the midbody. Interacts with ECT2; the interaction is detected at the midbody (By similarity).
Interacts with CCDC85B (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias, coiled coil, repeat.

TypeIDPosition(s)Description
Region1-32Disordered
Compositional bias10-32Polar residues
Coiled coil36-63
Region73-347Disordered
Compositional bias75-91Polar residues
Compositional bias106-279Polar residues
Compositional bias285-347Polar residues
Repeat517-556ARM 1
Repeat559-598ARM 2
Repeat603-643ARM 3
Compositional bias772-786Basic and acidic residues
Region772-809Disordered
Repeat861-900ARM 4

Sequence similarities

Belongs to the beta-catenin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q68FH0-1

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.

  • Length
    1,190
  • Mass (Da)
    131,551
  • Last updated
    2004-10-11 v1
  • Checksum
    DB6548B5EBE72CFE
MPAPEQGSLVEEGQPQTHQEAVSTGPGMEPETTATTILASVKEQELQFQRLTRELEVERQIVASQLERCRLGAESPSIASTSSTEKSFPWRSTDVPNPGVSKPRVSDTIHPNNYLIRTEPEQGTLYSPEQTSLHESEGSLGNSRSSTQMNSYSDSGYQEAGSFHNSQTVNKADSRQHPFTGSTSNHVVRTSRAEGQTLVQPSVANRAMRRVSSVPSRAQSPSYVTSTGVSPSRGSLRTSLGSGFGSPSVTDSRPLNPSAYSSSTLPAQRAASPYSQRPASPTAVRRVGSVTSRQTSNPNGPVPQYQTTTRVGSPLTLTDAQTRVASPSQGQVGSSSPKRSGMTAVPQHLGPSLQRTVHDMDQFGQQQYDIYERMVPPRPDSLTGLRSSYASQHSQLGQELRSAVSPDLHITPIYEGRTYYSPVYRSPNHGTVELQGSQTALYRTGSVGIGNLQRTSSQRSTLTYQRNNYALNTAATYAEPYRPVQYRVQECSYNRLQHTGPADDGATRSPSIDSIQKDPREFAWRDPELPEVIHMLQHQFPSVQANAAAYLQHLCFGDNKVKMEVYRLGGIKHLVDLLDHRVLEVQKNACGALRNLVFGKSTDENKIAMKNVGGIPALLRLLRKSIDAEVRELVTGVLWNLSSCDAVKMTIIRDALSTLTNTVIVPHSGWNNSSFDDDHKIKFQTSLVLRNTTGCLRNLSSAGEEARKQMRSCEGLVDSLLYVIHTCVNTSDYDSKTVENCVCTLRNLSYRLELEVPQARLLGLNELDDLLGKESPSKDSEPSCWGKKKKKKKRTPQEDQWDGVGPIPGLSKSPKGVEMLWHPSVVKPYLTLLAESSNPATLEGSAGSLQNLSAGNWKFAAYIRAAVRKEKGLPILVELLRMDNDRVVSSVATALRNMALDVRNKELIGKYAMRDLVNRLPGGNGPSILSDETVAAICCALHEVTSKNMENAKALADSGGIEKLVNITKGRGDRSSLKVVKAAAQVLNTLWQYRDLRSIYKKDGWNQNHFITPVSTLERDRFKSHPSLSTTNQQMSPIIQSVGSTSSSPALLGIREPRSEYDRTQPPMQYYNSQGDTTHKGLYPGSSKPSPIYISSYSSPAREQNRRLQHQQLYYQDDSTRKTLDAYRLYLQSPRSYEDPYCDDRVHFPASTDYSTQYGLKSTTNYVDFYSTKRPSYRAEQYPGSPDSWV

Q68FH0-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q68FH0-3

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
V9GXG7V9GXG7_MOUSEPkp4215
V9GWY7V9GWY7_MOUSEPkp446
A2AS44A2AS44_MOUSEPkp4803
A2AS45A2AS45_MOUSEPkp41163
A2AS47A2AS47_MOUSEPkp4849

Sequence caution

The sequence BAC37187.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for alternative sequence, compositional bias, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0123741-341in isoform 3
Compositional bias10-32Polar residues
Compositional bias75-91Polar residues
Compositional bias106-279Polar residues
Compositional bias285-347Polar residues
Sequence conflict328in Ref. 2; AAH78638
Alternative sequenceVSP_012375637in isoform 3
Alternative sequenceVSP_012376638-1190in isoform 3
Compositional bias772-786Basic and acidic residues
Sequence conflict877in Ref. 3; BAC36708
Alternative sequenceVSP_0123771042-1084in isoform 2
Sequence conflict1118in Ref. 3; BAC36708
Sequence conflict1161in Ref. 3; BAB32313

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL845536
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC078638
EMBL· GenBank· DDBJ
AAH78638.1
EMBL· GenBank· DDBJ
mRNA
BC079848
EMBL· GenBank· DDBJ
AAH79848.1
EMBL· GenBank· DDBJ
mRNA
BC082578
EMBL· GenBank· DDBJ
AAH82578.1
EMBL· GenBank· DDBJ
mRNA
AK021168
EMBL· GenBank· DDBJ
BAB32313.1
EMBL· GenBank· DDBJ
mRNA
AK077250
EMBL· GenBank· DDBJ
BAC36708.1
EMBL· GenBank· DDBJ
mRNA
AK078240
EMBL· GenBank· DDBJ
BAC37187.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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