dbPTM

MCRS1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MCRS1_HUMAN
UniProt AC	Q96EZ8
Protein Name	Microspherule protein 1
Gene Name	MCRS1
Organism	Homo sapiens (Human).
Sequence Length	462
Subcellular Localization	Nucleus . Nucleus, nucleolus . Cytoplasm . In microspherules in the nucleolus.
Protein Description	Modulates the transcription repressor activity of DAXX by recruiting it to the nucleolus. [PubMed: 11948183 As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues]
Protein Sequence	MDKDSQGLLDSSLMASGTASRSEDEESLAGQKRASSQALGTIPKRRSSSRFIKRKKFDDELVESSLAKSSTRAKGASGVEPGRCSGSEPSSSEKKKVSKAPSTPVPPSPAPAPGLTKRVKKSKQPLQVTKDLGRWKPADDLLLINAVLQTNDLTSVHLGVKFSCRFTLREVQERWYALLYDPVISKLACQAMRQLHPEAIAAIQSKALFSKAEEQLLSKVGSTSQPTLETFQDLLHRHPDAFYLARTAKALQAHWQLMKQYYLLEDQTVQPLPKGDQVLNFSDAEDLIDDSKLKDMRDEVLEHELMVADRRQKREIRQLEQELHKWQVLVDSITGMSSPDFDNQTLAVLRGRMVRYLMRSREITLGRATKDNQIDVDLSLEGPAWKISRKQGVIKLKNNGDFFIANEGRRPIYIDGRPVLCGSKWRLSNNSVVEIASLRFVFLINQDLIALIRAEAAKITPQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDKDSQGL -------CCCCCHHC	15.13	22814378
3 (in isoform 3)	Phosphorylation	-	58.96	25159151
5 (in isoform 3)	Phosphorylation	-	31.71	25159151
5	Phosphorylation	---MDKDSQGLLDSS ---CCCCCHHCCCHH	31.71	23403867
7 (in isoform 3)	Phosphorylation	-	31.96	25159151
8 (in isoform 2)	Phosphorylation	-	3.58	27251275
9 (in isoform 3)	Phosphorylation	-	8.41	25849741
11	Phosphorylation	DSQGLLDSSLMASGT CCHHCCCHHHHHCCC	25.91	28102081
12	Phosphorylation	SQGLLDSSLMASGTA CHHCCCHHHHHCCCC	23.10	28102081
14 (in isoform 2)	Phosphorylation	-	2.77	27251275
16	Phosphorylation	LDSSLMASGTASRSE CCHHHHHCCCCCCCC	23.78	25159151
18	Phosphorylation	SSLMASGTASRSEDE HHHHHCCCCCCCCCH	20.97	25159151
18 (in isoform 2)	Phosphorylation	-	20.97	27251275
20	Phosphorylation	LMASGTASRSEDEES HHHCCCCCCCCCHHH	35.86	25159151
22	Phosphorylation	ASGTASRSEDEESLA HCCCCCCCCCHHHHH	47.07	29255136
24 (in isoform 2)	Phosphorylation	-	67.23	27251275
27	Phosphorylation	SRSEDEESLAGQKRA CCCCCHHHHHHHHHH	22.82	22115753
32	Acetylation	EESLAGQKRASSQAL HHHHHHHHHHHHHHH	49.35	25953088
35	Phosphorylation	LAGQKRASSQALGTI HHHHHHHHHHHHCCC	27.32	25159151
36	Phosphorylation	AGQKRASSQALGTIP HHHHHHHHHHHCCCC	20.63	25159151
41	Phosphorylation	ASSQALGTIPKRRSS HHHHHHCCCCCCCCC	34.65	27794612
47	Phosphorylation	GTIPKRRSSSRFIKR CCCCCCCCCCCCCCC	36.38	26074081
48	Phosphorylation	TIPKRRSSSRFIKRK CCCCCCCCCCCCCCC	24.58	26074081
49	Phosphorylation	IPKRRSSSRFIKRKK CCCCCCCCCCCCCCC	32.24	26074081
56	Sumoylation	SRFIKRKKFDDELVE CCCCCCCCCCHHHHH	59.04	-
56	Sumoylation	SRFIKRKKFDDELVE CCCCCCCCCCHHHHH	59.04	-
64	Phosphorylation	FDDELVESSLAKSST CCHHHHHHHHHCCCC	24.15	28555341
65	Phosphorylation	DDELVESSLAKSSTR CHHHHHHHHHCCCCC	20.88	28555341
68	Acetylation	LVESSLAKSSTRAKG HHHHHHHCCCCCCCC	50.67	25953088
74	Methylation	AKSSTRAKGASGVEP HCCCCCCCCCCCCCC	52.28	116253419
77	Phosphorylation	STRAKGASGVEPGRC CCCCCCCCCCCCCCC	52.63	30177828
85	Phosphorylation	GVEPGRCSGSEPSSS CCCCCCCCCCCCCCH	43.95	29209046
87	Phosphorylation	EPGRCSGSEPSSSEK CCCCCCCCCCCCHHC	30.00	29209046
90	Phosphorylation	RCSGSEPSSSEKKKV CCCCCCCCCHHCCCC	42.31	29209046
91	Phosphorylation	CSGSEPSSSEKKKVS CCCCCCCCHHCCCCC	53.91	29209046
92	Phosphorylation	SGSEPSSSEKKKVSK CCCCCCCHHCCCCCC	58.74	28450419
98	Phosphorylation	SSEKKKVSKAPSTPV CHHCCCCCCCCCCCC	31.79	20860994
99	Acetylation	SEKKKVSKAPSTPVP HHCCCCCCCCCCCCC	68.27	25953088
102	Phosphorylation	KKVSKAPSTPVPPSP CCCCCCCCCCCCCCC	50.64	30266825
103	Phosphorylation	KVSKAPSTPVPPSPA CCCCCCCCCCCCCCC	27.52	29255136
108	Phosphorylation	PSTPVPPSPAPAPGL CCCCCCCCCCCCCCC	27.85	25159151
116	Phosphorylation	PAPAPGLTKRVKKSK CCCCCCCCCCHHHCC	23.79	23403867
117	Acetylation	APAPGLTKRVKKSKQ CCCCCCCCCHHHCCC	61.30	25953088
117	Ubiquitination	APAPGLTKRVKKSKQ CCCCCCCCCHHHCCC	61.30	-
121	Acetylation	GLTKRVKKSKQPLQV CCCCCHHHCCCCCEE	61.09	25953088
123	Acetylation	TKRVKKSKQPLQVTK CCCHHHCCCCCEEEC	65.89	19608861
130	Acetylation	KQPLQVTKDLGRWKP CCCCEEECCCCCCCC	52.69	19608861
130	Ubiquitination	KQPLQVTKDLGRWKP CCCCEEECCCCCCCC	52.69	19608861
136	Acetylation	TKDLGRWKPADDLLL ECCCCCCCCHHHEEE	29.03	19608861
143 (in isoform 2)	Ubiquitination	-	3.54	-
143	Acetylation	KPADDLLLINAVLQT CCHHHEEEEEEEECC	3.54	19608861
167	Phosphorylation	VKFSCRFTLREVQER CEEEEEEEHHHHHHH	12.93	24719451
198 (in isoform 3)	Ubiquitination	-	41.79	21906983
206 (in isoform 3)	Ubiquitination	-	32.50	21906983
206	Ubiquitination	AIAAIQSKALFSKAE HHHHHHHHHHHHHHH	32.50	-
210	Phosphorylation	IQSKALFSKAEEQLL HHHHHHHHHHHHHHH	31.63	24719451
211	Ubiquitination	QSKALFSKAEEQLLS HHHHHHHHHHHHHHH	53.11	21906983
211	Acetylation	QSKALFSKAEEQLLS HHHHHHHHHHHHHHH	53.11	26051181
211 (in isoform 1)	Ubiquitination	-	53.11	21906983
218	Phosphorylation	KAEEQLLSKVGSTSQ HHHHHHHHHHCCCCC	33.61	24719451
219	Ubiquitination	AEEQLLSKVGSTSQP HHHHHHHHHCCCCCC	51.05	21906983
219 (in isoform 1)	Ubiquitination	-	51.05	21906983
219 (in isoform 2)	Ubiquitination	-	51.05	-
224 (in isoform 2)	Ubiquitination	-	35.54	21906983
232 (in isoform 2)	Ubiquitination	-	48.11	21906983
267	Ubiquitination	QYYLLEDQTVQPLPK HHHCCCCCEECCCCC	33.91	-
282	Phosphorylation	GDQVLNFSDAEDLID CCEEECCCCHHHHCC	34.53	19664994
291	Phosphorylation	AEDLIDDSKLKDMRD HHHHCCHHHHHHHHH	35.82	23927012
292	Ubiquitination	EDLIDDSKLKDMRDE HHHCCHHHHHHHHHH	67.56	-
364	Phosphorylation	LMRSREITLGRATKD HHHCCCEEECCCCCC	20.57	24719451
369	Phosphorylation	EITLGRATKDNQIDV CEEECCCCCCCCCEE	37.25	23403867
370	Ubiquitination	ITLGRATKDNQIDVD EEECCCCCCCCCEEE	54.41	-
383 (in isoform 2)	Ubiquitination	-	26.10	-
390	Acetylation	PAWKISRKQGVIKLK CCEEEEECCCEEEEC	44.61	26051181
395	Acetylation	SRKQGVIKLKNNGDF EECCCEEEECCCCCE	51.51	26051181
397	Ubiquitination	KQGVIKLKNNGDFFI CCCEEEECCCCCEEE	43.28	-
410 (in isoform 2)	Ubiquitination	-	32.59	-
424	Acetylation	RPVLCGSKWRLSNNS EEEECCCEEECCCCC	22.93	26051181
458	Ubiquitination	LIRAEAAKITPQ--- HHHHHHHHCCCC---	54.91	-
460	Phosphorylation	RAEAAKITPQ----- HHHHHHCCCC-----	18.22	20860994
471 (in isoform 2)	Ubiquitination	-		-

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
35	S	Phosphorylation	Kinase	AURKA	O14965	GPS
36	S	Phosphorylation	Kinase	AURKA	O14965	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MCRS1_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 MCRS1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KXDL1_HUMAN	KXD1	physical	16189514
CEP44_HUMAN	CEP44	physical	16189514
RALYL_HUMAN	RALYL	physical	16189514
CC85B_HUMAN	CCDC85B	physical	16189514
MED4_HUMAN	MED4	physical	16189514
WASC3_HUMAN	CCDC53	physical	16189514
WBP11_HUMAN	WBP11	physical	16189514
CSK2B_HUMAN	CSNK2B	physical	17353931
UBR4_HUMAN	UBR4	physical	17353931
UBR5_HUMAN	UBR5	physical	17353931
KAP0_HUMAN	PRKAR1A	physical	17353931
TERT_HUMAN	TERT	physical	15044100
NOP2_HUMAN	NOP2	physical	9654073
FBRL_HUMAN	FBL	physical	9654073
DAXX_HUMAN	DAXX	physical	11948183
CHD4_HUMAN	CHD4	physical	16186106
RET_HUMAN	RET	physical	16186106
UBF1_HUMAN	UBTF	physical	16186106
RUVB1_HUMAN	RUVBL1	physical	17721549
RUVB2_HUMAN	RUVBL2	physical	17721549
ACL6A_HUMAN	ACTL6A	physical	17721549
IN80C_HUMAN	INO80C	physical	17721549
TYY1_HUMAN	YY1	physical	17721549
INO80_HUMAN	INO80	physical	17721549
NFRKB_HUMAN	NFRKB	physical	17721549
TFPT_HUMAN	TFPT	physical	17721549
ARP5_HUMAN	ACTR5	physical	17721549
ARP8_HUMAN	ACTR8	physical	17721549
IN80B_HUMAN	INO80B	physical	17721549
IN80E_HUMAN	INO80E	physical	17721549
UCHL5_HUMAN	UCHL5	physical	17721549
IN80D_HUMAN	INO80D	physical	17721549
UBR5_HUMAN	UBR5	physical	23069210
CC85B_HUMAN	CCDC85B	physical	17014843
M3K5_HUMAN	MAP3K5	physical	22609355
DAXX_HUMAN	DAXX	physical	22609355
WASC3_HUMAN	CCDC53	physical	19060904
GPBP1_HUMAN	GPBP1	physical	19060904
GCC1_HUMAN	GCC1	physical	19060904
KDM1A_HUMAN	KDM1A	physical	23455924
ANM5_HUMAN	PRMT5	physical	23455924
SUV91_HUMAN	SUV39H1	physical	23455924
WASC3_HUMAN	CCDC53	physical	25416956
USBP1_HUMAN	USHBP1	physical	25416956
K1958_HUMAN	KIAA1958	physical	25416956
BRCA1_HUMAN	BRCA1	physical	25184681
BAP1_HUMAN	BAP1	physical	26300492
PTEN_HUMAN	PTEN	physical	15659546

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 MCRS1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-123 AND LYS-130, AND MASSSPECTROMETRY.	19608861 [Abstract]
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-108 AND SER-282, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; THR-103 ANDSER-108, AND MASS SPECTROMETRY.	19413330 [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-103; SER-108 ANDSER-282, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND MASSSPECTROMETRY.	16565220 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-103 AND SER-108, ANDMASS SPECTROMETRY.	16964243 [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 SER-282, AND MASSSPECTROMETRY.	17081983 [Abstract]