dbPTM

MPP8_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MPP8_MOUSE
UniProt AC	Q3TYA6
Protein Name	M-phase phosphoprotein 8 {ECO:0000250\|UniProtKB:Q99549}
Gene Name	Mphosph8 {ECO:0000250\|UniProtKB:Q99549, ECO:0000312\|MGI:MGI:1922589}
Organism	Mus musculus (Mouse).
Sequence Length	858
Subcellular Localization	Nucleus . Chromosome . Detected on heterochromatin (PubMed:23416073). Dissociates from chromatin during interphase and early mitosis (PubMed:23416073). Detected on nucleosomes (By similarity).
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. Mediates recruitment of the HUSH complex to H3K9me3 sites: 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. Binds H3K9me and promotes DNA methylation by recruiting DNMT3A to target CpG sites; these can be situated within the coding region of the gene. Mediates down-regulation of CDH1 expression..
Protein Sequence	MAAAAEEGMSAAALVMSVPDSIGRSPESEGVGAGDEEKDAATKGTVAVGDSEEDGEDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRKKLAENKAKAVRKDIQRLSLNNDIFEADSDSDQQSDTKEDISPRKKKKKIKCKEETSPEDLRKKRTKMGKLKDKFKTELESTSEIIGFDVKTKKRIWEVKEELKDSKKPKKDEIKETKELKKANKRAEVRDLKIKIREDVKENRKTKKERYIESPLESESPNDSLILEDDSEDFISDNREENQNVRSVRDKTAQETVQEGIFEKHLDDLISIEEDAGTRVRRKKTKPRKFEEPKEIKKLESTNAFLERRAIPKKQRNQDKGISNLELNKLPSPVFAQTLKSSRLSGEEKSLKSPDLAEEEKEKKNEPKGKYQKRYDLDKEEKARKEPKVLKSFKEIRNAFDLFKKTTEEKNDVLENNSKREEISLDSKIMNDNKTKDKCSLKEKRNTRDETDTWAYIAAEGDQEVSDSVCQTDETSDGRQPVLSLGMDLQLEWMKLEDFQKHLDGEDEPFITTNRIPNNLLRDAVKNGDYIAVKVALNSNEEYNLDQEDSTGMTLVMLAAAGGQDDLLRLLITKGAKVNGRQKNGTTALIHAAEKNFLTTVAILLEAGAFVNVQQSNGETALMKACKRGNSDIVRLVIECGADCNILSKHQNSALYFAKQCNNVLVYELLKSHLETLSRVAEETIRDYFESRLALLEPVFPIACHRLCEGPDFSTDFNYMPPQNMPEGSGVLLFIFHANFLGKDVIARLCGPCSVQAVVLNDKFQLPVFLDSHFVYSFSPVAGPNKLFIRLTEAPFAKVKLLIGAYRVQLQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	AAAEEGMSAAALVMS HHHHHCCCHHHHHHC	26.13	25367039
17	Phosphorylation	SAAALVMSVPDSIGR CHHHHHHCCCCCCCC	24.02	20531401
21	Phosphorylation	LVMSVPDSIGRSPES HHHCCCCCCCCCCCC	22.37	23429704
25	Phosphorylation	VPDSIGRSPESEGVG CCCCCCCCCCCCCCC	28.01	23429704
28	Phosphorylation	SIGRSPESEGVGAGD CCCCCCCCCCCCCCH	42.93	23429704
42	Phosphorylation	DEEKDAATKGTVAVG HHHCCCCCCCEEEEC	31.56	25367039
45	Phosphorylation	KDAATKGTVAVGDSE CCCCCCCEEEECCCC	13.57	25619855
51	Phosphorylation	GTVAVGDSEEDGEDV CEEEECCCCCCCCCE	36.64	25521595
83	Phosphorylation	YKVRWKGYTSEDDTW EEEEECCCCCCCCCC	11.90	25521595
84	Phosphorylation	KVRWKGYTSEDDTWE EEEECCCCCCCCCCC	34.02	25521595
85	Phosphorylation	VRWKGYTSEDDTWEP EEECCCCCCCCCCCC	30.46	21082442
89	Phosphorylation	GYTSEDDTWEPEVHL CCCCCCCCCCCEECH	44.01	25521595
126	Phosphorylation	RKDIQRLSLNNDIFE HHHHHHHHCCCCCEE	31.10	22324799
136	Phosphorylation	NDIFEADSDSDQQSD CCCEECCCCCCCCCC	46.17	21082442
138	Phosphorylation	IFEADSDSDQQSDTK CEECCCCCCCCCCCC	41.07	21082442
142	Phosphorylation	DSDSDQQSDTKEDIS CCCCCCCCCCCCCCC	41.43	21082442
144	Phosphorylation	DSDQQSDTKEDISPR CCCCCCCCCCCCCHH	41.39	22324799
149	Phosphorylation	SDTKEDISPRKKKKK CCCCCCCCHHHHHCC	30.86	21149613
163	Phosphorylation	KIKCKEETSPEDLRK CCCCCCCCCHHHHHH	51.15	25619855
164	Phosphorylation	IKCKEETSPEDLRKK CCCCCCCCHHHHHHH	29.58	25619855
188	Phosphorylation	KFKTELESTSEIIGF HHHHHHHCCHHEECE	50.27	-
258	Phosphorylation	RKTKKERYIESPLES HCCHHHHHCCCCCCC	15.33	25293948
261	Phosphorylation	KKERYIESPLESESP HHHHHCCCCCCCCCC	25.81	25293948
265	Phosphorylation	YIESPLESESPNDSL HCCCCCCCCCCCCCE	51.57	21149613
267	Phosphorylation	ESPLESESPNDSLIL CCCCCCCCCCCCEEE	37.98	21149613
271	Phosphorylation	ESESPNDSLILEDDS CCCCCCCCEEECCCC	24.77	21149613
278	Phosphorylation	SLILEDDSEDFISDN CEEECCCCCCCCCCC	51.92	25293948
283	Phosphorylation	DDSEDFISDNREENQ CCCCCCCCCCHHHHC	28.91	30635358
303	Phosphorylation	RDKTAQETVQEGIFE HHHHHHHHHHHCHHH	18.53	-
318	Phosphorylation	KHLDDLISIEEDAGT HHHHHHHEHHCCCCC	31.11	-
325	Phosphorylation	SIEEDAGTRVRRKKT EHHCCCCCCCCCCCC	27.93	-
332	Phosphorylation	TRVRRKKTKPRKFEE CCCCCCCCCCCCCCC	49.68	-
379	Phosphorylation	LELNKLPSPVFAQTL HHHHCCCCHHHHHHH	44.10	25521595
385	Phosphorylation	PSPVFAQTLKSSRLS CCHHHHHHHHHCCCC	32.49	25159016
388	Phosphorylation	VFAQTLKSSRLSGEE HHHHHHHHCCCCCCC	24.65	22871156
392	Phosphorylation	TLKSSRLSGEEKSLK HHHHCCCCCCCHHCC	42.94	27149854
396	Acetylation	SRLSGEEKSLKSPDL CCCCCCCHHCCCCCH	57.71	6566037
397	Phosphorylation	RLSGEEKSLKSPDLA CCCCCCHHCCCCCHH	44.29	25777480
400	Phosphorylation	GEEKSLKSPDLAEEE CCCHHCCCCCHHHHH	29.01	25521595
453	Phosphorylation	AFDLFKKTTEEKNDV HHHHHHHCHHHHHHH	39.78	-
465	Phosphorylation	NDVLENNSKREEISL HHHHHCCCCCCEECC	44.67	22802335
471	Phosphorylation	NSKREEISLDSKIMN CCCCCEECCCHHHCC	29.42	23737553
474	Phosphorylation	REEISLDSKIMNDNK CCEECCCHHHCCCCC	29.40	23737553
714	Phosphorylation	QCNNVLVYELLKSHL HCCCHHHHHHHHHHH	9.19	-
738	Phosphorylation	TIRDYFESRLALLEP HHHHHHHHHHHHHHC	23.77	28285833

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
149	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot
164	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot
385	T	Phosphorylation	Kinase	CDK1	P11440	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MPP8_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 MPP8_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of MPP8_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MPP8_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-85, AND MASSSPECTROMETRY.	17242355 [Abstract]