PPHLN_MOUSE - dbPTM
PPHLN_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPHLN_MOUSE
UniProt AC Q8K2H1
Protein Name Periphilin-1 {ECO:0000250|UniProtKB:Q8NEY8}
Gene Name Pphln1 {ECO:0000312|MGI:MGI:1917029}
Organism Mus musculus (Mouse).
Sequence Length 381
Subcellular Localization Nucleus . Cytoplasm . Chromosome . 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 ju
Protein Description 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..
Protein Sequence MWSEGRYDYDRLPRERVPPRSHPSDGYHRVVNVVPKRPPLLDKRPPLLDKRPPLLARPDEGGYSRYYSHVDCRVCDEGRSFSHDRRSGPSHSGDESGYRWLRDDHSTSRQPDYRDMRDGFRRKSFYSSHYSRDRSPHKRDAPFFRESPVGRKDSPHSRSGSSVSSRSYSPERSRTHSFHQSQHRKSSRVGASYKRQNEAIRGRGKERSIQSVKTSRDASPSSSSAVASSKALDKPSRLTEKELAEAESKWANETLEKSDESNLAEMNEFEAGSTAPLFIDQTEEPESNTVDGTELYEDSQLSNRSKAIASKTKEIEQVYRQDCETFGMVVKMLIEKDPSLEKSVQFALRQNLHEIGERCVEELKRFITEYDNSARDFGDPF
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
87PhosphorylationSFSHDRRSGPSHSGD
CCCCCCCCCCCCCCC		56.8225159016
90PhosphorylationHDRRSGPSHSGDESG
CCCCCCCCCCCCCCC		33.5325159016
92PhosphorylationRRSGPSHSGDESGYR
CCCCCCCCCCCCCCC		52.8825159016
96PhosphorylationPSHSGDESGYRWLRD
CCCCCCCCCCCCCCC		45.9525159016
98PhosphorylationHSGDESGYRWLRDDH
CCCCCCCCCCCCCCC		14.1125159016
106PhosphorylationRWLRDDHSTSRQPDY
CCCCCCCCCCCCCCH		34.7625266776
124PhosphorylationRDGFRRKSFYSSHYS
HCCHHHHHHHHHCCC		27.8326239621
126PhosphorylationGFRRKSFYSSHYSRD
CHHHHHHHHHCCCCC		19.1628066266
127PhosphorylationFRRKSFYSSHYSRDR
HHHHHHHHHCCCCCC		14.5028066266
128PhosphorylationRRKSFYSSHYSRDRS
HHHHHHHHCCCCCCC		18.3126643407
130PhosphorylationKSFYSSHYSRDRSPH
HHHHHHCCCCCCCCC		13.8326643407
131PhosphorylationSFYSSHYSRDRSPHK
HHHHHCCCCCCCCCC		23.4526643407
135PhosphorylationSHYSRDRSPHKRDAP
HCCCCCCCCCCCCCC		35.3326643407
147PhosphorylationDAPFFRESPVGRKDS
CCCCCCCCCCCCCCC		22.1927087446
154PhosphorylationSPVGRKDSPHSRSGS
CCCCCCCCCCCCCCC		27.7823140645
162PhosphorylationPHSRSGSSVSSRSYS
CCCCCCCCCCCCCCC		29.5523984901
164PhosphorylationSRSGSSVSSRSYSPE
CCCCCCCCCCCCCCC		23.2123984901
165PhosphorylationRSGSSVSSRSYSPER
CCCCCCCCCCCCCCC		24.0823984901
167PhosphorylationGSSVSSRSYSPERSR
CCCCCCCCCCCCCCC		31.7323984901
168PhosphorylationSSVSSRSYSPERSRT
CCCCCCCCCCCCCCC		27.4323984901
169PhosphorylationSVSSRSYSPERSRTH
CCCCCCCCCCCCCCC		22.8725159016
175PhosphorylationYSPERSRTHSFHQSQ
CCCCCCCCCCCHHHH		24.1028066266
177PhosphorylationPERSRTHSFHQSQHR
CCCCCCCCCHHHHHH		24.6623684622
181PhosphorylationRTHSFHQSQHRKSSR
CCCCCHHHHHHHHCC		21.2727149854
201MethylationKRQNEAIRGRGKERS
HHHHHHHCCCCCCHH		35.4930988919
208PhosphorylationRGRGKERSIQSVKTS
CCCCCCHHHHHCCCC		26.5225159016
211PhosphorylationGKERSIQSVKTSRDA
CCCHHHHHCCCCCCC		24.7426239621
214PhosphorylationRSIQSVKTSRDASPS
HHHHHCCCCCCCCCC		27.1725521595
215PhosphorylationSIQSVKTSRDASPSS
HHHHCCCCCCCCCCC		23.5727087446
219PhosphorylationVKTSRDASPSSSSAV
CCCCCCCCCCCHHHH		29.6027087446
221PhosphorylationTSRDASPSSSSAVAS
CCCCCCCCCHHHHHH		40.1225521595
222PhosphorylationSRDASPSSSSAVASS
CCCCCCCCHHHHHHH		31.5327742792
223PhosphorylationRDASPSSSSAVASSK
CCCCCCCHHHHHHHC		27.0128833060
224PhosphorylationDASPSSSSAVASSKA
CCCCCCHHHHHHHCC		28.8028833060
228PhosphorylationSSSSAVASSKALDKP
CCHHHHHHHCCCCCC		26.2728833060
229PhosphorylationSSSAVASSKALDKPS
CHHHHHHHCCCCCCC		16.5328833060
249AcetylationELAEAESKWANETLE
HHHHHHHHHHHHHHH		41.66-
319PhosphorylationTKEIEQVYRQDCETF
HHHHHHHHHHHHHHH		11.4022817900
339PhosphorylationMLIEKDPSLEKSVQF
HHHHCCCCHHHHHHH		60.3322817900
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PPHLN_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPHLN_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PPHLN_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PPHLN_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PPHLN_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147; SER-169 ANDSER-219, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND MASSSPECTROMETRY.

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