PPHLN_MOUSE
ID PPHLN_MOUSE Reviewed; 381 AA.
AC Q8K2H1; Q8BUZ6;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Periphilin-1 {ECO:0000250|UniProtKB:Q8NEY8};
GN Name=Pphln1 {ECO:0000312|MGI:MGI:1917029};
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19621438; DOI=10.1002/dvg.20553;
RA Soehn A.S., Pham T.T., Schaeferhoff K., Floss T., Weisenhorn D.M.,
RA Wurst W., Bonin M., Riess O.;
RT "Periphilin is strongly expressed in the murine nervous system and is
RT indispensable for murine development.";
RL Genesis 47:697-707(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
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: Component of the HUSH complex, a multiprotein complex that
CC mediates epigenetic repression. The HUSH complex is recruited to
CC genomic loci rich in H3K9me3 and is probably required to maintain
CC transcriptional silencing by promoting recruitment of SETDB1, a histone
CC methyltransferase that mediates further deposition of H3K9me3. In the
CC HUSH complex, contributes to the maintenance of the complex at
CC chromatin. Acts as a transcriptional corepressor and regulates the cell
CC cycle, probably via the HUSH complex. The HUSH complex is also involved
CC in the silencing of unintegrated retroviral DNA: some part of the
CC retroviral DNA formed immediately after infection remains unintegrated
CC in the host genome and is transcriptionally repressed. May be involved
CC in epithelial differentiation by contributing to epidermal integrity
CC and barrier formation. {ECO:0000250|UniProtKB:Q8NEY8}.
CC -!- SUBUNIT: Homodimer (By similarity). Component of the HUSH complex; at
CC least composed of TASOR, PPHLN1 and MPHOSPH8 (By similarity). Interacts
CC with SIN3A and HDAC1 (By similarity). May interact with PPL (By
CC similarity). {ECO:0000250|UniProtKB:Q8NEY8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NEY8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8NEY8}. Chromosome
CC {ECO:0000250|UniProtKB:Q8NEY8}. Note=In undifferentiated keratinocytes
CC expressed in speckle-type nuclear granules and at the nuclear membrane,
CC but in the differentiated keratinocytes colocalized with periplakin at
CC the cell periphery and at cell-cell junctions. Localizes to chromatin.
CC {ECO:0000250|UniProtKB:Q8NEY8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K2H1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K2H1-2; Sequence=VSP_009908;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Strong expression in the
CC developing somites and limbs, the embryonic nervous system and the
CC adult brain. {ECO:0000269|PubMed:19621438}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality. Embryos die during early
CC embryogenesis. {ECO:0000269|PubMed:19621438}.
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DR EMBL; AK081606; BAC38270.1; -; mRNA.
DR EMBL; BC031486; AAH31486.3; -; mRNA.
DR CCDS; CCDS27767.1; -. [Q8K2H1-1]
DR CCDS; CCDS27768.1; -. [Q8K2H1-2]
DR RefSeq; NP_780572.1; NM_175363.4.
DR RefSeq; XP_006520920.1; XM_006520857.1.
DR AlphaFoldDB; Q8K2H1; -.
DR SMR; Q8K2H1; -.
DR BioGRID; 230202; 8.
DR IntAct; Q8K2H1; 1.
DR STRING; 10090.ENSMUSP00000042762; -.
DR iPTMnet; Q8K2H1; -.
DR PhosphoSitePlus; Q8K2H1; -.
DR jPOST; Q8K2H1; -.
DR MaxQB; Q8K2H1; -.
DR PaxDb; Q8K2H1; -.
DR PeptideAtlas; Q8K2H1; -.
DR PRIDE; Q8K2H1; -.
DR ProteomicsDB; 291782; -. [Q8K2H1-1]
DR ProteomicsDB; 291783; -. [Q8K2H1-2]
DR DNASU; 223828; -.
DR GeneID; 223828; -.
DR KEGG; mmu:223828; -.
DR CTD; 51535; -.
DR MGI; MGI:1917029; Pphln1.
DR eggNOG; ENOG502QW3I; Eukaryota.
DR InParanoid; Q8K2H1; -.
DR OrthoDB; 924482at2759; -.
DR PhylomeDB; Q8K2H1; -.
DR BioGRID-ORCS; 223828; 9 hits in 71 CRISPR screens.
DR ChiTaRS; Pphln1; mouse.
DR PRO; PR:Q8K2H1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8K2H1; protein.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0097355; P:protein localization to heterochromatin; ISS:UniProtKB.
DR InterPro; IPR028851; Pphln1.
DR PANTHER; PTHR15836; PTHR15836; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosome; Cytoplasm; Isopeptide bond;
KW Keratinization; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..381
FT /note="Periphilin-1"
FT /id="PRO_0000058538"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 117..123
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY8"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY8"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY8"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY8"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY8"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY8"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY8"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 249
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY8"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY8"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY8"
FT CROSSLNK 194
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY8"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY8"
FT CROSSLNK 241
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY8"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY8"
FT CROSSLNK 342
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY8"
FT VAR_SEQ 25..93
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009908"
FT CONFLICT 375
FT /note="R -> Q (in Ref. 1; BAC38270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 43835 MW; 90C3AC70BA644D77 CRC64;
MWSEGRYDYD RLPRERVPPR SHPSDGYHRV VNVVPKRPPL LDKRPPLLDK RPPLLARPDE
GGYSRYYSHV DCRVCDEGRS FSHDRRSGPS HSGDESGYRW LRDDHSTSRQ PDYRDMRDGF
RRKSFYSSHY SRDRSPHKRD APFFRESPVG RKDSPHSRSG SSVSSRSYSP ERSRTHSFHQ
SQHRKSSRVG ASYKRQNEAI RGRGKERSIQ SVKTSRDASP SSSSAVASSK ALDKPSRLTE
KELAEAESKW ANETLEKSDE SNLAEMNEFE AGSTAPLFID QTEEPESNTV DGTELYEDSQ
LSNRSKAIAS KTKEIEQVYR QDCETFGMVV KMLIEKDPSL EKSVQFALRQ NLHEIGERCV
EELKRFITEY DNSARDFGDP F
