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Protein

Periphilin-1

Gene

Pphln1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression. The HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3. In the HUSH complex, contributes to the maintenance of the complex at chromatin. Acts as a transcriptional corepressor and regulates the cell cycle, probably via the HUSH complex. May be involved in epithelial differentiation by contributing to epidermal integrity and barrier formation.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Keratinization, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Periphilin-1By similarity
Gene namesi
Name:Pphln1Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1917029. Pphln1.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity
  • Chromosome By similarity

  • Note: In undifferentiated keratinocytes expressed in speckle-type nuclear granules and at the nuclear membrane, but in the differentiated keratinocytes colocalized with periplakin at the cell periphery and at cell-cell junctions. Localizes to chromatin.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality. Embryos die during early embryogenesis.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 381381Periphilin-1PRO_0000058538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei124 – 1241PhosphoserineBy similarity
Modified residuei128 – 1281PhosphoserineBy similarity
Modified residuei147 – 1471PhosphoserineBy similarity
Modified residuei154 – 1541PhosphoserineBy similarity
Modified residuei181 – 1811PhosphoserineBy similarity
Modified residuei211 – 2111PhosphoserineBy similarity
Modified residuei215 – 2151PhosphoserineBy similarity
Modified residuei219 – 2191PhosphoserineCombined sources
Modified residuei249 – 2491N6-acetyllysineBy similarity
Modified residuei339 – 3391PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8K2H1.
MaxQBiQ8K2H1.
PaxDbiQ8K2H1.
PeptideAtlasiQ8K2H1.
PRIDEiQ8K2H1.

PTM databases

iPTMnetiQ8K2H1.
PhosphoSiteiQ8K2H1.

Miscellaneous databases

PMAP-CutDBQ8K2H1.

Expressioni

Tissue specificityi

Ubiquitously expressed. Strong expression in the developing somites and limbs, the embryonic nervous system and the adult brain.1 Publication

Gene expression databases

CleanExiMM_PPHLN1.

Interactioni

Subunit structurei

Homodimer. Component of the HUSH complex; at least composed of FAM208A/TASOR, PPHLN1 and MPHOSPH8. Interacts with SIN3A and HDAC1. Interacts with PPL.By similarity

Protein-protein interaction databases

BioGridi230202. 3 interactions.
IntActiQ8K2H1. 1 interaction.
STRINGi10090.ENSMUSP00000042762.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi117 – 1237Nuclear localization signalBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi154 – 22976Ser-richAdd
BLAST

Phylogenomic databases

eggNOGiENOG410IFSB. Eukaryota.
ENOG4111JYA. LUCA.
HOGENOMiHOG000074159.
HOVERGENiHBG053653.
InParanoidiQ8K2H1.
PhylomeDBiQ8K2H1.

Family and domain databases

InterProiIPR028851. Pphln1.
[Graphical view]
PANTHERiPTHR15836:SF2. PTHR15836:SF2. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8K2H1-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MWSEGRYDYD RLPRERVPPR SHPSDGYHRV VNVVPKRPPL LDKRPPLLDK
60 70 80 90 100
RPPLLARPDE GGYSRYYSHV DCRVCDEGRS FSHDRRSGPS HSGDESGYRW
110 120 130 140 150
LRDDHSTSRQ PDYRDMRDGF RRKSFYSSHY SRDRSPHKRD APFFRESPVG
160 170 180 190 200
RKDSPHSRSG SSVSSRSYSP ERSRTHSFHQ SQHRKSSRVG ASYKRQNEAI
210 220 230 240 250
RGRGKERSIQ SVKTSRDASP SSSSAVASSK ALDKPSRLTE KELAEAESKW
260 270 280 290 300
ANETLEKSDE SNLAEMNEFE AGSTAPLFID QTEEPESNTV DGTELYEDSQ
310 320 330 340 350
LSNRSKAIAS KTKEIEQVYR QDCETFGMVV KMLIEKDPSL EKSVQFALRQ
360 370 380
NLHEIGERCV EELKRFITEY DNSARDFGDP F
Note: No experimental confirmation available.
Length:381
Mass (Da):43,835
Last modified:October 1, 2002 - v1
Checksum:i90C3AC70BA644D77
GO
Isoform 2 (identifier: Q8K2H1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     25-93: Missing.

Note: No experimental confirmation available.
Show »
Length:312
Mass (Da):35,985
Checksum:i0FCE5AA9928B753E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti375 – 3751R → Q in BAC38270 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei25 – 9369Missing in isoform 2. 1 PublicationVSP_009908Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK081606 mRNA. Translation: BAC38270.1.
BC031486 mRNA. Translation: AAH31486.3.
CCDSiCCDS27767.1. [Q8K2H1-1]
CCDS27768.1. [Q8K2H1-2]
RefSeqiNP_780572.1. NM_175363.4.
XP_006520920.1. XM_006520857.1.
UniGeneiMm.74208.

Genome annotation databases

GeneIDi223828.
KEGGimmu:223828.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK081606 mRNA. Translation: BAC38270.1.
BC031486 mRNA. Translation: AAH31486.3.
CCDSiCCDS27767.1. [Q8K2H1-1]
CCDS27768.1. [Q8K2H1-2]
RefSeqiNP_780572.1. NM_175363.4.
XP_006520920.1. XM_006520857.1.
UniGeneiMm.74208.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230202. 3 interactions.
IntActiQ8K2H1. 1 interaction.
STRINGi10090.ENSMUSP00000042762.

PTM databases

iPTMnetiQ8K2H1.
PhosphoSiteiQ8K2H1.

Proteomic databases

EPDiQ8K2H1.
MaxQBiQ8K2H1.
PaxDbiQ8K2H1.
PeptideAtlasiQ8K2H1.
PRIDEiQ8K2H1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi223828.
KEGGimmu:223828.

Organism-specific databases

CTDi51535.
MGIiMGI:1917029. Pphln1.

Phylogenomic databases

eggNOGiENOG410IFSB. Eukaryota.
ENOG4111JYA. LUCA.
HOGENOMiHOG000074159.
HOVERGENiHBG053653.
InParanoidiQ8K2H1.
PhylomeDBiQ8K2H1.

Miscellaneous databases

ChiTaRSiPphln1. mouse.
PMAP-CutDBQ8K2H1.
PROiQ8K2H1.
SOURCEiSearch...

Gene expression databases

CleanExiMM_PPHLN1.

Family and domain databases

InterProiIPR028851. Pphln1.
[Graphical view]
PANTHERiPTHR15836:SF2. PTHR15836:SF2. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Embryonic head.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Mammary gland.
  3. "Periphilin is strongly expressed in the murine nervous system and is indispensable for murine development."
    Soehn A.S., Pham T.T., Schaeferhoff K., Floss T., Weisenhorn D.M., Wurst W., Bonin M., Riess O.
    Genesis 47:697-707(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiPPHLN_MOUSE
AccessioniPrimary (citable) accession number: Q8K2H1
Secondary accession number(s): Q8BUZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2002
Last modified: July 6, 2016
This is version 94 of the entry and version 1 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.