dbPTM

MPH6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MPH6_HUMAN
UniProt AC	Q99547
Protein Name	M-phase phosphoprotein 6
Gene Name	MPHOSPH6
Organism	Homo sapiens (Human).
Sequence Length	160
Subcellular Localization	Nucleus, nucleolus. Cytoplasm. Cytoplasmic in M phase.
Protein Description	RNA-binding protein that associates with the RNA exosome complex. Involved in the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA and may play a role in recruiting the RNA exosome complex to pre-rRNA; this function may include C1D..
Protein Sequence	MAAERKTRLSKNLLRMKFMQRGLDSETKKQLEEEEKKIISEEHWYLDLPELKEKESFIIEEQSFLLCEDLLYGRMSFRGFNPEVEKLMLQMNAKHKAEEVEDETVELDVSDEEMARRYETLVGTIGKKFARKRDHANYEEDENGDITPIKAKKMFLKPQD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Ubiquitination	ERKTRLSKNLLRMKF HHHHHHHHHHHHHHH	57.09	-
11	Sumoylation	ERKTRLSKNLLRMKF HHHHHHHHHHHHHHH	57.09	-
11	Sumoylation	ERKTRLSKNLLRMKF HHHHHHHHHHHHHHH	57.09	-
17	Acetylation	SKNLLRMKFMQRGLD HHHHHHHHHHHCCCC	31.11	24468261
17	Ubiquitination	SKNLLRMKFMQRGLD HHHHHHHHHHHCCCC	31.11	-
25	Phosphorylation	FMQRGLDSETKKQLE HHHCCCCHHHHHHHH	52.81	21712546
27	Phosphorylation	QRGLDSETKKQLEEE HCCCCHHHHHHHHHH	47.71	29083192
37	Sumoylation	QLEEEEKKIISEEHW HHHHHHHHHCCCHHH	48.85	28112733
45	Phosphorylation	IISEEHWYLDLPELK HCCCHHHCCCCHHHH	7.70	27642862
52	Ubiquitination	YLDLPELKEKESFII CCCCHHHHHHHCEEE	66.14	-
54	Ubiquitination	DLPELKEKESFIIEE CCHHHHHHHCEEECH	58.01	-
76	Phosphorylation	DLLYGRMSFRGFNPE HHHHCCCCCCCCCHH	15.49	24719451
86	Sumoylation	GFNPEVEKLMLQMNA CCCHHHHHHHHHHHH	44.35	28112733
86	Ubiquitination	GFNPEVEKLMLQMNA CCCHHHHHHHHHHHH	44.35	21906983
96	Ubiquitination	LQMNAKHKAEEVEDE HHHHHHCCCHHHCCC	57.71	-
104	Phosphorylation	AEEVEDETVELDVSD CHHHCCCCEEECCCH	31.44	30266825
110	Phosphorylation	ETVELDVSDEEMARR CCEEECCCHHHHHHH	38.68	30266825
118	Phosphorylation	DEEMARRYETLVGTI HHHHHHHHHHHHHHH	14.01	28796482
120	Phosphorylation	EMARRYETLVGTIGK HHHHHHHHHHHHHHH	20.15	23312004
124	Phosphorylation	RYETLVGTIGKKFAR HHHHHHHHHHHHHHH	21.05	25159151
127	Ubiquitination	TLVGTIGKKFARKRD HHHHHHHHHHHHHCC	40.65	21906983
127	Acetylation	TLVGTIGKKFARKRD HHHHHHHHHHHHHCC	40.65	25953088
127	2-Hydroxyisobutyrylation	TLVGTIGKKFARKRD HHHHHHHHHHHHHCC	40.65	-
127	Sumoylation	TLVGTIGKKFARKRD HHHHHHHHHHHHHCC	40.65	28112733
128	Ubiquitination	LVGTIGKKFARKRDH HHHHHHHHHHHHCCC	38.76	-
132	Ubiquitination	IGKKFARKRDHANYE HHHHHHHHCCCCCCC	59.76	-
138	Phosphorylation	RKRDHANYEEDENGD HHCCCCCCCCCCCCC	22.83	27642862
147	Phosphorylation	EDENGDITPIKAKKM CCCCCCCCCCCCCCC	24.57	22167270
150	Sumoylation	NGDITPIKAKKMFLK CCCCCCCCCCCCCCC	56.19	28112733
150	Ubiquitination	NGDITPIKAKKMFLK CCCCCCCCCCCCCCC	56.19	21906983
150	Acetylation	NGDITPIKAKKMFLK CCCCCCCCCCCCCCC	56.19	25953088
150	Sumoylation	NGDITPIKAKKMFLK CCCCCCCCCCCCCCC	56.19	-
153	Sumoylation	ITPIKAKKMFLKPQD CCCCCCCCCCCCCCC	39.48	25772364
153	Ubiquitination	ITPIKAKKMFLKPQD CCCCCCCCCCCCCCC	39.48	-
153	Methylation	ITPIKAKKMFLKPQD CCCCCCCCCCCCCCC	39.48	110868535
153	Sumoylation	ITPIKAKKMFLKPQD CCCCCCCCCCCCCCC	39.48	-
157	Ubiquitination	KAKKMFLKPQD---- CCCCCCCCCCC----	29.39	-
157	Acetylation	KAKKMFLKPQD---- CCCCCCCCCCC----	29.39	22424773

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 MPH6_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MPH6_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 MPH6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ERG28_HUMAN	C14orf1	physical	16169070
APLP1_HUMAN	APLP1	physical	16169070
RBM48_HUMAN	RBM48	physical	16169070
GDF9_HUMAN	GDF9	physical	16169070
LRIF1_HUMAN	LRIF1	physical	16169070
U119A_HUMAN	UNC119	physical	16169070
ZHX1_HUMAN	ZHX1	physical	16169070
TLE1_HUMAN	TLE1	physical	16169070
P53_HUMAN	TP53	physical	16169070
PRPF3_HUMAN	PRPF3	physical	22939629
EXOSX_HUMAN	EXOSC10	physical	26344197
EXOS2_HUMAN	EXOSC2	physical	26344197
EXOS3_HUMAN	EXOSC3	physical	26344197
EXOS4_HUMAN	EXOSC4	physical	26344197
EXOS6_HUMAN	EXOSC6	physical	26344197
EXOS9_HUMAN	EXOSC9	physical	28877463
EXOS7_HUMAN	EXOSC7	physical	28877463
EXOS8_HUMAN	EXOSC8	physical	28877463
EXOS3_HUMAN	EXOSC3	physical	28877463
EXOS2_HUMAN	EXOSC2	physical	28877463
EXOS6_HUMAN	EXOSC6	physical	28877463
EXOS5_HUMAN	EXOSC5	physical	28877463
EXOS4_HUMAN	EXOSC4	physical	28877463
EXOS1_HUMAN	EXOSC1	physical	28877463

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 MPH6_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-110 AND THR-147, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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 THR-147, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147, AND MASSSPECTROMETRY.	18691976 [Abstract]
"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 THR-147, AND MASSSPECTROMETRY.	17081983 [Abstract]