PHC3_MOUSE - dbPTM
PHC3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHC3_MOUSE
UniProt AC Q8CHP6
Protein Name Polyhomeotic-like protein 3
Gene Name Phc3
Organism Mus musculus (Mouse).
Sequence Length 981
Subcellular Localization Nucleus.
Protein Description Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (By similarity)..
Protein Sequence MDSEPSSGTSVSTTASSTTTTTITTSSSRMQQPQISVYSGSDRHAVQVIQQALHRPPSSAAQYLQQMYAAQQQHLMLHTAALQQQHLSSSQLQSLAAVQASLSSGRPSTSPTGSVTQQSSMSQTSILSASPAPAQLMNRSQTSSSTSGSITQQTMLLGSTSPTLTASQAQMYLRAQMLIFTPATTVAAVQSDIPVVSSSPSPSCQSAAAQVQNLTLRSQKLGVLSSSQNGSPKSAGQTQSLTICHNKTTVTSSKISQRDPSPESKKGGSPGLESRSTAVTRTSSIHQLIAPASYSPIQPHSLIKHQQIPLHSPPPKVSHHQLLLQQQQQQIQPITLQSPSQDPPPSQHCIPLPNHGLSPAPSNAQPQHCSPVQSHPPPLTVSPNQAQSAQQSVVVSPPPPHSPSQSPTIIIHPQALIQPHPLVSSALQTGPNLQQAAADQVQSTAQLNLPSHLPLPASPVVHIGPVQQSALVSPGQQMVSPTSHQQYSALQSSPIPIATPPQMSASPPAQLPPLPLQSMQSLQVQPEILSQGQVLVQNALVSEEELPAAEALVQLPFQTLPPPQTVAVNLQVQPPAPVDPPVVYQVEDVCEEEMPEESDECARMDRTPPPPTLSPAAVTVGRGEDLTSEHPLLEQVELPAVASVSASVIKSPSDPTHASAPAPPLLIPAASTRSSSTSLASSTPSLENKPPQAIVKPQILTHVIEGFVIQEGLEPFPVSRSSLLIEQPVKKRPLLDNQVVNSVCVQPELQNNTKHADNSSDTEIEDMMAEETLEEMDSELLKCEFCGKMGYPNEFLRSKRFCTMSCAKRYNVSCSKKFALSRWNRKPDNQSLGHRGRRPSGPEGAAREHILRQLPITYPSAEEDVASHEDPVPSAMTTRLRRQSERERERELRDVRIRKMPENSDLLPVAQTEPSIWTVDDVWAFIHSLPGCQDVADEFRAQEIDGQALLLLKEDHLMSAMNMKLGPALKICARINSLKDS
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
3Phosphorylation-----MDSEPSSGTS
-----CCCCCCCCCC		50.5428576409
225PhosphorylationSQKLGVLSSSQNGSP
HHHHHCEECCCCCCC		26.0723984901
226PhosphorylationQKLGVLSSSQNGSPK
HHHHCEECCCCCCCC		31.6127087446
227PhosphorylationKLGVLSSSQNGSPKS
HHHCEECCCCCCCCC		25.0426643407
231PhosphorylationLSSSQNGSPKSAGQT
EECCCCCCCCCCCCC		36.3825521595
238O-linked_GlycosylationSPKSAGQTQSLTICH
CCCCCCCCCEEEEEE		21.1430059200
238PhosphorylationSPKSAGQTQSLTICH
CCCCCCCCCEEEEEE		21.14-
254AcetylationKTTVTSSKISQRDPS
CCEECCCCCCCCCCC		46.2522826441
261PhosphorylationKISQRDPSPESKKGG
CCCCCCCCHHHCCCC		45.6626824392
264PhosphorylationQRDPSPESKKGGSPG
CCCCCHHHCCCCCCC		42.9528833060
269PhosphorylationPESKKGGSPGLESRS
HHHCCCCCCCCHHCC		25.1825521595
273PhosphorylationKGGSPGLESRSTAVT
CCCCCCCHHCCCCEE		50.4424719451
274PhosphorylationGGSPGLESRSTAVTR
CCCCCCHHCCCCEEC		36.2525521595
281PhosphorylationSRSTAVTRTSSIHQL
HCCCCEECCCCCHHH		26.4724719451
282PhosphorylationRSTAVTRTSSIHQLI
CCCCEECCCCCHHHH		19.9123984901
283PhosphorylationSTAVTRTSSIHQLIA
CCCEECCCCCHHHHC		24.8123984901
284PhosphorylationTAVTRTSSIHQLIAP
CCEECCCCCHHHHCC		24.3926643407
293PhosphorylationHQLIAPASYSPIQPH
HHHHCCCCCCCCCCC		25.6926745281
294PhosphorylationQLIAPASYSPIQPHS
HHHCCCCCCCCCCCC		22.1426745281
295PhosphorylationLIAPASYSPIQPHSL
HHCCCCCCCCCCCCC		17.0326745281
301PhosphorylationYSPIQPHSLIKHQQI
CCCCCCCCCCCCCCC		38.1726745281
305PhosphorylationQPHSLIKHQQIPLHS
CCCCCCCCCCCCCCC		20.1324719451
312PhosphorylationHQQIPLHSPPPKVSH
CCCCCCCCCCCCCCH		46.9526824392
335PhosphorylationQQQIQPITLQSPSQD
HHHCCCCCCCCCCCC		25.9825338131
604OxidationESDECARMDRTPPPP
CCHHHHCCCCCCCCC		1.8617242355
607PhosphorylationECARMDRTPPPPTLS
HHHCCCCCCCCCCCC		35.5625521595
612PhosphorylationDRTPPPPTLSPAAVT
CCCCCCCCCCCCEEE		45.7125521595
614PhosphorylationTPPPPTLSPAAVTVG
CCCCCCCCCCEEEEC		18.2525521595
619PhosphorylationTLSPAAVTVGRGEDL
CCCCCEEEECCCCCC		16.7125619855
651PhosphorylationVSASVIKSPSDPTHA
EEEECCCCCCCCCCC		20.6426643407
653PhosphorylationASVIKSPSDPTHASA
EECCCCCCCCCCCCC		64.4126643407
656PhosphorylationIKSPSDPTHASAPAP
CCCCCCCCCCCCCCC		34.7626643407
659PhosphorylationPSDPTHASAPAPPLL
CCCCCCCCCCCCCEE		27.4726643407
674PhosphorylationIPAASTRSSSTSLAS
EECCCCCCCCCCCCC		28.8229472430
675PhosphorylationPAASTRSSSTSLASS
ECCCCCCCCCCCCCC		34.0529472430
676PhosphorylationAASTRSSSTSLASST
CCCCCCCCCCCCCCC		24.2229472430
677PhosphorylationASTRSSSTSLASSTP
CCCCCCCCCCCCCCC		29.7029472430
678PhosphorylationSTRSSSTSLASSTPS
CCCCCCCCCCCCCCC		24.7229472430
681PhosphorylationSSSTSLASSTPSLEN
CCCCCCCCCCCCCCC		39.7829472430
721PhosphorylationEPFPVSRSSLLIEQP
CCCCCCHHHEEEECC		20.1729176673
722PhosphorylationPFPVSRSSLLIEQPV
CCCCCHHHEEEECCC		26.5329176673
759PhosphorylationNTKHADNSSDTEIED
CCCCCCCCCCHHHHH		30.0921082442
760PhosphorylationTKHADNSSDTEIEDM
CCCCCCCCCHHHHHH		55.6021082442
762PhosphorylationHADNSSDTEIEDMMA
CCCCCCCHHHHHHHH		40.5926239621
772PhosphorylationEDMMAEETLEEMDSE
HHHHHHHHHHHHCHH		30.8629899451
826AcetylationALSRWNRKPDNQSLG
HHHHCCCCCCCCCCC		54.21155411
835MethylationDNQSLGHRGRRPSGP
CCCCCCCCCCCCCCC		38.2226542075
840PhosphorylationGHRGRRPSGPEGAAR
CCCCCCCCCCHHHHH		66.2325266776
858PhosphorylationLRQLPITYPSAEEDV
HHHCCCCCCCHHHHH		8.9126745281
860PhosphorylationQLPITYPSAEEDVAS
HCCCCCCCHHHHHHC		37.5926745281
867PhosphorylationSAEEDVASHEDPVPS
CHHHHHHCCCCCCCC		27.5329514104
884PhosphorylationTTRLRRQSERERERE
HHHHHHHHHHHHHHH		36.4923684622
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 PHC3_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHC3_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 PHC3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BMI1_MOUSEBmi1physical
17001316
CBX2_MOUSECbx2physical
17001316
TYY1_MOUSEYy1physical
17001316
E2F6_MOUSEE2f6physical
17001316
SOX9_MOUSESox9physical
17001316
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PHC3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-269; THR-607 ANDSER-614, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; THR-607 ANDSER-614, AND MASS SPECTROMETRY.

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