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PKP1_MOUSE
ID   PKP1_MOUSE              Reviewed;         728 AA.
AC   P97350; B2RSX3;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Plakophilin-1;
GN   Name=Pkp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RA   Nimmrich V., Hunziker A.H., Franke W.W.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-143, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Liver, and Pancreas;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Seems to play a role in junctional plaques. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cell junction, desmosome
CC       {ECO:0000250}. Note=Nuclear and associated with desmosomes.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
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DR   EMBL; Y07941; CAA69240.1; -; mRNA.
DR   EMBL; BC139041; AAI39042.1; -; mRNA.
DR   EMBL; BC139042; AAI39043.1; -; mRNA.
DR   CCDS; CCDS15322.1; -.
DR   RefSeq; NP_001300630.1; NM_001313701.1.
DR   RefSeq; NP_062619.1; NM_019645.3.
DR   AlphaFoldDB; P97350; -.
DR   SMR; P97350; -.
DR   BioGRID; 202212; 16.
DR   IntAct; P97350; 9.
DR   MINT; P97350; -.
DR   STRING; 10090.ENSMUSP00000027667; -.
DR   iPTMnet; P97350; -.
DR   PhosphoSitePlus; P97350; -.
DR   EPD; P97350; -.
DR   MaxQB; P97350; -.
DR   PaxDb; P97350; -.
DR   PeptideAtlas; P97350; -.
DR   PRIDE; P97350; -.
DR   ProteomicsDB; 289441; -.
DR   Antibodypedia; 20641; 211 antibodies from 20 providers.
DR   DNASU; 18772; -.
DR   Ensembl; ENSMUST00000027667; ENSMUSP00000027667; ENSMUSG00000026413.
DR   Ensembl; ENSMUST00000163260; ENSMUSP00000128418; ENSMUSG00000026413.
DR   GeneID; 18772; -.
DR   KEGG; mmu:18772; -.
DR   UCSC; uc007cub.1; mouse.
DR   CTD; 5317; -.
DR   MGI; MGI:1328359; Pkp1.
DR   VEuPathDB; HostDB:ENSMUSG00000026413; -.
DR   eggNOG; KOG1048; Eukaryota.
DR   GeneTree; ENSGT00940000156735; -.
DR   HOGENOM; CLU_009111_3_1_1; -.
DR   InParanoid; P97350; -.
DR   OMA; SYYTKTQ; -.
DR   OrthoDB; 765704at2759; -.
DR   PhylomeDB; P97350; -.
DR   TreeFam; TF321877; -.
DR   Reactome; R-MMU-351906; Apoptotic cleavage of cell adhesion proteins.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-6805567; Keratinization.
DR   Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR   BioGRID-ORCS; 18772; 0 hits in 73 CRISPR screens.
DR   ChiTaRS; Pkp1; mouse.
DR   PRO; PR:P97350; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P97350; protein.
DR   Bgee; ENSMUSG00000026413; Expressed in tail skin and 78 other tissues.
DR   ExpressionAtlas; P97350; baseline and differential.
DR   Genevisible; P97350; MM.
DR   GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR   GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030057; C:desmosome; IDA:MGI.
DR   GO; GO:1990124; C:messenger ribonucleoprotein complex; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR   GO; GO:0005521; F:lamin binding; ISO:MGI.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR   GO; GO:0045110; P:intermediate filament bundle assembly; ISO:MGI.
DR   GO; GO:1902373; P:negative regulation of mRNA catabolic process; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR028432; Plakophilin-1.
DR   InterPro; IPR028435; Plakophilin/d_Catenin.
DR   PANTHER; PTHR10372; PTHR10372; 1.
DR   PANTHER; PTHR10372:SF3; PTHR10372:SF3; 1.
DR   Pfam; PF00514; Arm; 2.
DR   SMART; SM00185; ARM; 7.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 3.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell junction; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat.
FT   CHAIN           1..728
FT                   /note="Plakophilin-1"
FT                   /id="PRO_0000064285"
FT   REPEAT          244..275
FT                   /note="ARM 1"
FT   REPEAT          276..317
FT                   /note="ARM 2"
FT   REPEAT          318..360
FT                   /note="ARM 3"
FT   REPEAT          361..412
FT                   /note="ARM 4"
FT   REPEAT          413..443
FT                   /note="ARM 5"
FT   REPEAT          505..536
FT                   /note="ARM 6"
FT   REPEAT          537..583
FT                   /note="ARM 7"
FT   REPEAT          584..629
FT                   /note="ARM 8"
FT   REPEAT          630..694
FT                   /note="ARM 9"
FT   REGION          48..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         122
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   728 AA;  80896 MW;  BDAC5BA7B4118AC0 CRC64;
     MNHSPLKTAL AYECFQDQDN STLALPSDQK MKTGTSGRQR VQEQVMMTVK RQKSKSSQSS
     TLSHSNRGSM YDGLADNYNN YGTTSRSSYF SKFQAGNGSW GYPIYNGTLK REPDNRRFSS
     YSQMENWSRH YPRGSCATPG AGSDICFMQK IKASRSEPDL YCDPRGTLRK GTLGSKGHKT
     TQNRCSFYST CSGQKAVKKC PVRPPSCTSK QDPVYVPPIS CNKDLSFGHS RASSKICSED
     IECSGLTIPK AVQYLCSQDE KYQAIGAYYI QHTCFQDESA KQQVYQLGGI CKLVDLLRSP
     NQNVQQAAAG ALRNLVFRST PNKLETRRQN GIREAVSLLR RSGSTEIQKQ LTGLLWNLSS
     TDELKEELVA DALPVLTDRV IIPFSGWCDG NSNMSREVVD PEVFFNATGC LRNLSSADAG
     RQTMRNYSGL IDSLMAYVQN CVAASRCDDK SVENCMCILH NLSYRLDAEV PTRYRQLEYN
     TRNAYTEKSS TGCFSNRGDK MMNNNYDCPL PEEETNPKGS SWLYHSDAIR TYLNLMGKSK
     KDATLEACAG ALQNLTASKG LMSNGMSQLI GIKEKGLPQI ARLLQSGNSD VVRSGASLLS
     NMSRHPVLHR VMGNQVFPEV TRLLTSHTGN TSNSEDILSS ACYTVRNLMT SQPQMAKQYF
     SNSMLNNVFN LCRNTASSPK AAEAARLLLS DMWASKELQS VLRQQGFDRN MMGNIAGANN
     LRNFTSRF
 
 
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