Q68FH0 · PKP4_MOUSE
- ProteinPlakophilin-4
- GenePkp4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1190 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | adherens junction | |
Cellular Component | cell-cell contact zone | |
Cellular Component | cell-cell junction | |
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic side of plasma membrane | |
Cellular Component | cytoskeleton | |
Cellular Component | desmosome | |
Cellular Component | midbody | |
Cellular Component | mitotic spindle | |
Cellular Component | nucleus | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | plasma membrane | |
Cellular Component | postsynaptic density | |
Cellular Component | spindle midzone | |
Cellular Component | spindle pole | |
Molecular Function | cadherin binding | |
Biological Process | cell-cell adhesion | |
Biological Process | cell-cell junction assembly | |
Biological Process | positive regulation of cytokinesis | |
Biological Process | positive regulation of GTPase activity |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePlakophilin-4
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ68FH0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000064290 | 1-1190 | Plakophilin-4 | |||
Sequence: MPAPEQGSLVEEGQPQTHQEAVSTGPGMEPETTATTILASVKEQELQFQRLTRELEVERQIVASQLERCRLGAESPSIASTSSTEKSFPWRSTDVPNPGVSKPRVSDTIHPNNYLIRTEPEQGTLYSPEQTSLHESEGSLGNSRSSTQMNSYSDSGYQEAGSFHNSQTVNKADSRQHPFTGSTSNHVVRTSRAEGQTLVQPSVANRAMRRVSSVPSRAQSPSYVTSTGVSPSRGSLRTSLGSGFGSPSVTDSRPLNPSAYSSSTLPAQRAASPYSQRPASPTAVRRVGSVTSRQTSNPNGPVPQYQTTTRVGSPLTLTDAQTRVASPSQGQVGSSSPKRSGMTAVPQHLGPSLQRTVHDMDQFGQQQYDIYERMVPPRPDSLTGLRSSYASQHSQLGQELRSAVSPDLHITPIYEGRTYYSPVYRSPNHGTVELQGSQTALYRTGSVGIGNLQRTSSQRSTLTYQRNNYALNTAATYAEPYRPVQYRVQECSYNRLQHTGPADDGATRSPSIDSIQKDPREFAWRDPELPEVIHMLQHQFPSVQANAAAYLQHLCFGDNKVKMEVYRLGGIKHLVDLLDHRVLEVQKNACGALRNLVFGKSTDENKIAMKNVGGIPALLRLLRKSIDAEVRELVTGVLWNLSSCDAVKMTIIRDALSTLTNTVIVPHSGWNNSSFDDDHKIKFQTSLVLRNTTGCLRNLSSAGEEARKQMRSCEGLVDSLLYVIHTCVNTSDYDSKTVENCVCTLRNLSYRLELEVPQARLLGLNELDDLLGKESPSKDSEPSCWGKKKKKKKRTPQEDQWDGVGPIPGLSKSPKGVEMLWHPSVVKPYLTLLAESSNPATLEGSAGSLQNLSAGNWKFAAYIRAAVRKEKGLPILVELLRMDNDRVVSSVATALRNMALDVRNKELIGKYAMRDLVNRLPGGNGPSILSDETVAAICCALHEVTSKNMENAKALADSGGIEKLVNITKGRGDRSSLKVVKAAAQVLNTLWQYRDLRSIYKKDGWNQNHFITPVSTLERDRFKSHPSLSTTNQQMSPIIQSVGSTSSSPALLGIREPRSEYDRTQPPMQYYNSQGDTTHKGLYPGSSKPSPIYISSYSSPAREQNRRLQHQQLYYQDDSTRKTLDAYRLYLQSPRSYEDPYCDDRVHFPASTDYSTQYGLKSTTNYVDFYSTKRPSYRAEQYPGSPDSWV | ||||||
Modified residue | 75 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 84 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 106 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 132 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 136 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 139 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 220 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 230 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 235 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 253 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 269 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 272 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 280 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 313 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 326 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 336 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 371 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 391 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 402 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 405 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 411 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 414 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 421 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 426 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 437 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 477 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 509 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 511 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 514 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 775 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1012 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1016 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1044 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1090 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1099 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1133 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
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).
Interacts with CCDC85B (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-32 | Disordered | ||||
Sequence: MPAPEQGSLVEEGQPQTHQEAVSTGPGMEPET | ||||||
Compositional bias | 10-32 | Polar residues | ||||
Sequence: VEEGQPQTHQEAVSTGPGMEPET | ||||||
Coiled coil | 36-63 | |||||
Sequence: TILASVKEQELQFQRLTRELEVERQIVA | ||||||
Region | 73-347 | Disordered | ||||
Sequence: AESPSIASTSSTEKSFPWRSTDVPNPGVSKPRVSDTIHPNNYLIRTEPEQGTLYSPEQTSLHESEGSLGNSRSSTQMNSYSDSGYQEAGSFHNSQTVNKADSRQHPFTGSTSNHVVRTSRAEGQTLVQPSVANRAMRRVSSVPSRAQSPSYVTSTGVSPSRGSLRTSLGSGFGSPSVTDSRPLNPSAYSSSTLPAQRAASPYSQRPASPTAVRRVGSVTSRQTSNPNGPVPQYQTTTRVGSPLTLTDAQTRVASPSQGQVGSSSPKRSGMTAVPQ | ||||||
Compositional bias | 75-91 | Polar residues | ||||
Sequence: SPSIASTSSTEKSFPWR | ||||||
Compositional bias | 106-279 | Polar residues | ||||
Sequence: SDTIHPNNYLIRTEPEQGTLYSPEQTSLHESEGSLGNSRSSTQMNSYSDSGYQEAGSFHNSQTVNKADSRQHPFTGSTSNHVVRTSRAEGQTLVQPSVANRAMRRVSSVPSRAQSPSYVTSTGVSPSRGSLRTSLGSGFGSPSVTDSRPLNPSAYSSSTLPAQRAASPYSQRPA | ||||||
Compositional bias | 285-347 | Polar residues | ||||
Sequence: RRVGSVTSRQTSNPNGPVPQYQTTTRVGSPLTLTDAQTRVASPSQGQVGSSSPKRSGMTAVPQ | ||||||
Repeat | 517-556 | ARM 1 | ||||
Sequence: KDPREFAWRDPELPEVIHMLQHQFPSVQANAAAYLQHLCF | ||||||
Repeat | 559-598 | ARM 2 | ||||
Sequence: NKVKMEVYRLGGIKHLVDLLDHRVLEVQKNACGALRNLVF | ||||||
Repeat | 603-643 | ARM 3 | ||||
Sequence: DENKIAMKNVGGIPALLRLLRKSIDAEVRELVTGVLWNLSS | ||||||
Compositional bias | 772-786 | Basic and acidic residues | ||||
Sequence: GKESPSKDSEPSCWG | ||||||
Region | 772-809 | Disordered | ||||
Sequence: GKESPSKDSEPSCWGKKKKKKKRTPQEDQWDGVGPIPG | ||||||
Repeat | 861-900 | ARM 4 | ||||
Sequence: AYIRAAVRKEKGLPILVELLRMDNDRVVSSVATALRNMAL |
Sequence similarities
Belongs to the beta-catenin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
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.
- Name1
- Length1,190
- Mass (Da)131,551
- Last updated2004-10-11 v1
- ChecksumDB6548B5EBE72CFE
Q68FH0-2
- Name2
- Differences from canonical
- 1042-1084: Missing
Q68FH0-3
- Name3
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_012374 | 1-341 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 10-32 | Polar residues | ||||
Sequence: VEEGQPQTHQEAVSTGPGMEPET | ||||||
Compositional bias | 75-91 | Polar residues | ||||
Sequence: SPSIASTSSTEKSFPWR | ||||||
Compositional bias | 106-279 | Polar residues | ||||
Sequence: SDTIHPNNYLIRTEPEQGTLYSPEQTSLHESEGSLGNSRSSTQMNSYSDSGYQEAGSFHNSQTVNKADSRQHPFTGSTSNHVVRTSRAEGQTLVQPSVANRAMRRVSSVPSRAQSPSYVTSTGVSPSRGSLRTSLGSGFGSPSVTDSRPLNPSAYSSSTLPAQRAASPYSQRPA | ||||||
Compositional bias | 285-347 | Polar residues | ||||
Sequence: RRVGSVTSRQTSNPNGPVPQYQTTTRVGSPLTLTDAQTRVASPSQGQVGSSSPKRSGMTAVPQ | ||||||
Sequence conflict | 328 | in Ref. 2; AAH78638 | ||||
Sequence: S → F | ||||||
Alternative sequence | VSP_012375 | 637 | in isoform 3 | |||
Sequence: V → G | ||||||
Alternative sequence | VSP_012376 | 638-1190 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 772-786 | Basic and acidic residues | ||||
Sequence: GKESPSKDSEPSCWG | ||||||
Sequence conflict | 877 | in Ref. 3; BAC36708 | ||||
Sequence: V → A | ||||||
Alternative sequence | VSP_012377 | 1042-1084 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 1118 | in Ref. 3; BAC36708 | ||||
Sequence: D → G | ||||||
Sequence conflict | 1161 | in Ref. 3; BAB32313 | ||||
Sequence: K → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |