MPP8_HUMAN - dbPTM
MPP8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MPP8_HUMAN
UniProt AC Q99549
Protein Name M-phase phosphoprotein 8
Gene Name MPHOSPH8 {ECO:0000312|HGNC:HGNC:29810}
Organism Homo sapiens (Human).
Sequence Length 860
Subcellular Localization Nucleus . Chromosome . Detected on heterochromatin (PubMed:20871592, PubMed:26022416). Dissociates from chromatin during interphase and early mitosis (PubMed:23416073). Detected on nucleosomes (PubMed:20871592).
Protein Description Heterochromatin component that specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes recruitment of proteins that mediate epigenetic repression. [PubMed: 20871592]
Protein Sequence MEQVAEGARVTAVPVSAADSTEELAEVEEGVGVVGEDNDAAARGAEAFGDSEEDGEDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRKKIAENKAKAVRKDIQRLSLNNDIFEANSDSDQQSETKEDTSPKKKKKKLRQREEKSPDDLKKKKAKAGKLKDKSKPDLESSLESLVFDLRTKKRISEAKEELKESKKPKKDEVKETKELKKVKKGEIRDLKTKTREDPKENRKTKKEKFVESQVESESSVLNDSPFPEDDSEGLHSDSREEKQNTKSARERAGQDMGLEHGFEKPLDSAMSAEEDTDVRGRRKKKTPRKAEDTRENRKLENKNAFLEKKTVPKKQRNQDRSKSAAELEKLMPVSAQTPKGRRLSGEERGLWSTDSAEEDKETKRNESKEKYQKRHDSDKEEKGRKEPKGLKTLKEIRNAFDLFKLTPEEKNDVSENNRKREEIPLDFKTIDDHKTKENKQSLKERRNTRDETDTWAYIAAEGDQEVLDSVCQADENSDGRQQILSLGMDLQLEWMKLEDFQKHLDGKDENFAATDAIPSNVLRDAVKNGDYITVKVALNSNEEYNLDQEDSSGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALHFAKQSNNVLVYDLLKNHLETLSRVAEETIKDYFEARLALLEPVFPIACHRLCEGPDFSTDFNYKPPQNIPEGSGILLFIFHANFLGKEVIARLCGPCSVQAVVLNDKFQLPVFLDSHFVYSFSPVAGPNKLFIRLTEAPSAKVKLLIGAYRVQLQ
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
1Acetylation-------MEQVAEGA
-------CCCCCCCC		7.9922814378
11PhosphorylationVAEGARVTAVPVSAA
CCCCCEEEEEECCCC		19.1827251275
16PhosphorylationRVTAVPVSAADSTEE
EEEEEECCCCCCHHH		16.2130624053
20PhosphorylationVPVSAADSTEELAEV
EECCCCCCHHHHHHH		32.7521712546
21PhosphorylationPVSAADSTEELAEVE
ECCCCCCHHHHHHHH		33.7426657352
51PhosphorylationGAEAFGDSEEDGEDV
HHHHHCCCCCCCCCC		43.1719664994
69PhosphorylationEKILDMKTEGGKVLY
EEEEEEEECCCEEEE		32.9722468782
73AcetylationDMKTEGGKVLYKVRW
EEEECCCEEEEEEEE		39.6723749302
83PhosphorylationYKVRWKGYTSDDDTW
EEEEECCCCCCCCCC		10.1922167270
84PhosphorylationKVRWKGYTSDDDTWE
EEEECCCCCCCCCCC		34.0622167270
85PhosphorylationVRWKGYTSDDDTWEP
EEECCCCCCCCCCCC		30.4722167270
89PhosphorylationGYTSDDDTWEPEIHL
CCCCCCCCCCCEECH		38.4330266825
126PhosphorylationRKDIQRLSLNNDIFE
HHHHHHHHCCCCCHH		31.1030266825
136PhosphorylationNDIFEANSDSDQQSE
CCCHHCCCCCHHHCC		45.6023927012
138PhosphorylationIFEANSDSDQQSETK
CHHCCCCCHHHCCCC		36.8225159151
142PhosphorylationNSDSDQQSETKEDTS
CCCCHHHCCCCCCCC		41.4226503892
144PhosphorylationDSDQQSETKEDTSPK
CCHHHCCCCCCCCHH		45.0130266825
148PhosphorylationQSETKEDTSPKKKKK
HCCCCCCCCHHHHHH		48.2830266825
149PhosphorylationSETKEDTSPKKKKKK
CCCCCCCCHHHHHHH		47.2230266825
163AcetylationKLRQREEKSPDDLKK
HHHHHHHCCHHHHHH		63.64129067
164PhosphorylationLRQREEKSPDDLKKK
HHHHHHCCHHHHHHH		36.5223401153
169AcetylationEKSPDDLKKKKAKAG
HCCHHHHHHHHHHHC		70.3390897
170AcetylationKSPDDLKKKKAKAGK
CCHHHHHHHHHHHCC		67.8090901
171AcetylationSPDDLKKKKAKAGKL
CHHHHHHHHHHHCCC		57.27129071
172AcetylationPDDLKKKKAKAGKLK
HHHHHHHHHHHCCCC		65.0919608861
177AcetylationKKKAKAGKLKDKSKP
HHHHHHCCCCCCCCC		58.1719608861
181UbiquitinationKAGKLKDKSKPDLES
HHCCCCCCCCCCHHH		59.8129967540
182PhosphorylationAGKLKDKSKPDLESS
HCCCCCCCCCCHHHH		60.6024732914
183UbiquitinationGKLKDKSKPDLESSL
CCCCCCCCCCHHHHH		48.5729967540
188PhosphorylationKSKPDLESSLESLVF
CCCCCHHHHHHHHHH		47.7425159151
189PhosphorylationSKPDLESSLESLVFD
CCCCHHHHHHHHHHH		27.1225159151
192PhosphorylationDLESSLESLVFDLRT
CHHHHHHHHHHHHHH		34.8222617229
204PhosphorylationLRTKKRISEAKEELK
HHHHHHHHHHHHHHH		35.2229214152
251AcetylationEDPKENRKTKKEKFV
CCHHHCHHCHHHHHH		76.0412436591
260PhosphorylationKKEKFVESQVESESS
HHHHHHHHHHHCCCC		33.9430108239
264PhosphorylationFVESQVESESSVLND
HHHHHHHCCCCCCCC		43.8730108239
266PhosphorylationESQVESESSVLNDSP
HHHHHCCCCCCCCCC		34.7230576142
267PhosphorylationSQVESESSVLNDSPF
HHHHCCCCCCCCCCC		26.9426657352
272PhosphorylationESSVLNDSPFPEDDS
CCCCCCCCCCCCCCC		27.6330266825
279PhosphorylationSPFPEDDSEGLHSDS
CCCCCCCCCCCCCCC		45.9830266825
284PhosphorylationDDSEGLHSDSREEKQ
CCCCCCCCCCHHHHH		42.1830266825
286PhosphorylationSEGLHSDSREEKQNT
CCCCCCCCHHHHHCH		44.6025849741
316PhosphorylationGFEKPLDSAMSAEED
CCCCCHHHCCCCCCC		33.2923401153
319PhosphorylationKPLDSAMSAEEDTDV
CCHHHCCCCCCCCCC		32.0423401153
324PhosphorylationAMSAEEDTDVRGRRK
CCCCCCCCCCCCCCC		39.4129255136
334PhosphorylationRGRRKKKTPRKAEDT
CCCCCCCCCCCHHHH		36.8923416073
358PhosphorylationNAFLEKKTVPKKQRN
HHHHHHCCCCHHHCC		53.7820068231
369PhosphorylationKQRNQDRSKSAAELE
HHCCCHHHHCHHHHH		38.9726657352
371PhosphorylationRNQDRSKSAAELEKL
CCCHHHHCHHHHHHH		33.6830576142
382PhosphorylationLEKLMPVSAQTPKGR
HHHHCCCCCCCCCCC		14.5930576142
385PhosphorylationLMPVSAQTPKGRRLS
HCCCCCCCCCCCCCC		27.0425159151
387UbiquitinationPVSAQTPKGRRLSGE
CCCCCCCCCCCCCCC		69.3229967540
392PhosphorylationTPKGRRLSGEERGLW
CCCCCCCCCCCCCCC		42.2020164059
400PhosphorylationGEERGLWSTDSAEED
CCCCCCCCCCCHHHH		27.6423927012
401PhosphorylationEERGLWSTDSAEEDK
CCCCCCCCCCHHHHH		23.5322167270
403PhosphorylationRGLWSTDSAEEDKET
CCCCCCCCHHHHHHH		37.3522167270
410PhosphorylationSAEEDKETKRNESKE
CHHHHHHHHHHHHHH		40.8323927012
415PhosphorylationKETKRNESKEKYQKR
HHHHHHHHHHHHHHH		50.0623312004
425PhosphorylationKYQKRHDSDKEEKGR
HHHHHCCCHHHHHCC		44.4430576142
436MethylationEKGRKEPKGLKTLKE
HHCCCCCCHHHHHHH		77.34-
439AcetylationRKEPKGLKTLKEIRN
CCCCCHHHHHHHHHH		61.5581418819
440PhosphorylationKEPKGLKTLKEIRNA
CCCCHHHHHHHHHHH		48.3725599653
452UbiquitinationRNAFDLFKLTPEEKN
HHHHHHHCCCHHHHC		59.7629967540
454PhosphorylationAFDLFKLTPEEKNDV
HHHHHCCCHHHHCCC		29.2830266825
458UbiquitinationFKLTPEEKNDVSENN
HCCCHHHHCCCCCCH		57.7033845483
476UbiquitinationEEIPLDFKTIDDHKT
CCCCCCCCCCCCCCC		44.2129967540
489PhosphorylationKTKENKQSLKERRNT
CCHHHHHHHHHHHCC		42.9123532336
496PhosphorylationSLKERRNTRDETDTW
HHHHHHCCCCHHHHH		37.3727422710
500PhosphorylationRRNTRDETDTWAYIA
HHCCCCHHHHHHHHE		42.9126657352
502PhosphorylationNTRDETDTWAYIAAE
CCCCHHHHHHHHEEC		21.2929116813
505PhosphorylationDETDTWAYIAAEGDQ
CHHHHHHHHEECCCH		5.2227251275
550UbiquitinationMKLEDFQKHLDGKDE
EEHHHHHHHCCCCCC		46.2433845483
555AcetylationFQKHLDGKDENFAAT
HHHHCCCCCCCCHHC		62.6326051181
555UbiquitinationFQKHLDGKDENFAAT
HHHHCCCCCCCCHHC		62.6329967540
567PhosphorylationAATDAIPSNVLRDAV
HHCCCCCHHHHHHHH		33.20-
575UbiquitinationNVLRDAVKNGDYITV
HHHHHHHHCCCEEEE		57.86-
623UbiquitinationLLRLLITKGAKVNGR
HHHHHHHCCCEECCC		50.2927667366
698AcetylationADCNILSKHQNSALH
CCCCCCCCCCCCHHH		45.8526051181
708UbiquitinationNSALHFAKQSNNVLV
CCHHHHHHHCCCEEH		54.0022817900
708 (in isoform 1)Ubiquitination-54.0021890473
708 (in isoform 2)Ubiquitination-54.0021890473
708AcetylationNSALHFAKQSNNVLV
CCHHHHHHHCCCEEH		54.0026051181
716 (in isoform 2)Phosphorylation-9.1925147952
716PhosphorylationQSNNVLVYDLLKNHL
HCCCEEHHHHHHHHH		9.1925839225
720UbiquitinationVLVYDLLKNHLETLS
EEHHHHHHHHHHHHH		50.01-
735UbiquitinationRVAEETIKDYFEARL
HHHHHHHHHHHHHHH		54.52-
841PhosphorylationNKLFIRLTEAPSAKV
CEEEEEEECCCCHHH		21.9120068231
845PhosphorylationIRLTEAPSAKVKLLI
EEEECCCCHHHHEEE		48.0125690035
847UbiquitinationLTEAPSAKVKLLIGA
EECCCCHHHHEEEEE		44.2122817900
849 (in isoform 1)Ubiquitination-36.5521890473
849UbiquitinationEAPSAKVKLLIGAYR
CCCCHHHHEEEEEEE		36.5522817900
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
149SPhosphorylationKinaseCDK1P06493
Uniprot
164SPhosphorylationKinaseCDK1P06493
Uniprot
334TPhosphorylationKinaseCDK1P06493
Uniprot
385TPhosphorylationKinaseCDK1P06493
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MPP8_HUMAN !!
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 MPP8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DNM3A_HUMANDNMT3Aphysical
22086334
EHMT1_HUMANEHMT1physical
22086334
MPP8_HUMANMPHOSPH8physical
22086334
ERCC6_HUMANERCC6physical
26496610
HCFC1_HUMANHCFC1physical
26496610
ILF3_HUMANILF3physical
26496610
NOP2_HUMANNOP2physical
26496610
NUMA1_HUMANNUMA1physical
26496610
RL24_HUMANRPL24physical
26496610
RT12_HUMANMRPS12physical
26496610
RS11_HUMANRPS11physical
26496610
SAFB1_HUMANSAFBphysical
26496610
UBF1_HUMANUBTFphysical
26496610
ZN121_HUMANZNF121physical
26496610
BRPF1_HUMANBRPF1physical
26496610
TRRAP_HUMANTRRAPphysical
26496610
SAFB2_HUMANSAFB2physical
26496610
MATR3_HUMANMATR3physical
26496610
TBCD4_HUMANTBC1D4physical
26496610
KHDR1_HUMANKHDRBS1physical
26496610
HECW1_HUMANHECW1physical
26496610
ANKL2_HUMANANKLE2physical
26496610
TASOR_HUMANFAM208Aphysical
26496610
RL36_HUMANRPL36physical
26496610
FBXL6_HUMANFBXL6physical
26496610
ZN638_HUMANZNF638physical
26496610
RM18_HUMANMRPL18physical
26496610
PPHLN_HUMANPPHLN1physical
26496610
F208B_HUMANFAM208Bphysical
26496610
ZN770_HUMANZNF770physical
26496610
PHIP_HUMANPHIPphysical
26496610
TMM33_HUMANTMEM33physical
26496610
IMP3_HUMANIMP3physical
26496610
DDX28_HUMANDDX28physical
26496610
ESYT2_HUMANESYT2physical
26496610
NCOA5_HUMANNCOA5physical
26496610
EHMT1_HUMANEHMT1physical
26496610
DLRB1_HUMANDYNLRB1physical
26496610
UTP23_HUMANUTP23physical
26496610
MCRI2_HUMANFAM195Aphysical
26496610
SPIR2_HUMANSPIRE2physical
26496610
USMG5_HUMANUSMG5physical
26496610
ZN845_HUMANZNF845physical
26496610
CGAS_HUMANMB21D1physical
26496610
TSR3_HUMANTSR3physical
26496610
RP25L_HUMANRPP25Lphysical
26496610
LRWD1_HUMANLRWD1physical
26496610
SIR1_HUMANSIRT1physical
25870236
H31_HUMANHIST1H3Aphysical
25870236
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MPP8_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-51, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-177, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-136; SER-138;SER-149; SER-188; SER-189; SER-192 AND SER-403, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-51, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-136; SER-138;SER-149; SER-189 AND THR-454, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-136; SER-138;SER-164; SER-319 AND SER-392, AND MASS SPECTROMETRY.

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