dbPTM

MSL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MSL2_HUMAN
UniProt AC	Q9HCI7
Protein Name	E3 ubiquitin-protein ligase MSL2
Gene Name	MSL2
Organism	Homo sapiens (Human).
Sequence Length	577
Subcellular Localization
Protein Description	Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at lysine 16 which is implicated in the formation of higher-order chromatin structure. Acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. This activity is greatly enhanced by heterodimerization with MSL1. H2B ubiquitination in turn stimulates histine H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1..
Protein Sequence	MNPVNATALYISASRLVLNYDPGDPKAFTEINRLLPYFRQSLSCCVCGHLLQDPIAPTNSTCQHYVCKTCKGKKMMMKPSCSWCKDYEQFEENKQLSILVNCYKKLCEYITQTTLARDIIEAVDCSSDILALLNDGSLFCEETEKPSDSSFTLCLTHSPLPSTSEPTTDPQASLSPMSESTLSIAIGSSVINGLPTYNGLSIDRFGINIPSPEHSNTIDVCNTVDIKTEDLSDSLPPVCDTVATDLCSTGIDICSFSEDIKPGDSLLLSVEEVLRSLETVSNTEVCCPNLQPNLEATVSNGPFLQLSSQSLSHNVFMSTSPALHGLSCTAATPKIAKLNRKRSRSESDSEKVQPLPISTIIRGPTLGASAPVTVKRESKISLQPIATVPNGGTTPKISKTVLLSTKSMKKSHEHGSKKSHSKTKPGILKKDKAVKEKIPSHHFMPGSPTKTVYKKPQEKKGCKCGRATQNPSVLTCRGQRCPCYSNRKACLDCICRGCQNSYMANGEKKLEAFAVPEKALEQTRLTLGINVTSIAVRNASTSTSVINVTGSPVTTFLAASTHDDKSLDEAIDMRFDC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MNPVNATALYISAS -CCCCCHHHEEEEHH	16.40	23663014
10	Phosphorylation	PVNATALYISASRLV CCCHHHEEEEHHEEE	7.14	23663014
12	Phosphorylation	NATALYISASRLVLN CHHHEEEEHHEEECC	13.46	23663014
14	Phosphorylation	TALYISASRLVLNYD HHEEEEHHEEECCCC	21.25	23663014
20	Ubiquitination	ASRLVLNYDPGDPKA HHEEECCCCCCCHHH	21.25	29967540
20	Phosphorylation	ASRLVLNYDPGDPKA HHEEECCCCCCCHHH	21.25	19605366
26	Ubiquitination	NYDPGDPKAFTEINR CCCCCCHHHHHHHHH	61.95	-
29	Phosphorylation	PGDPKAFTEINRLLP CCCHHHHHHHHHHHH	40.59	-
78	Acetylation	KGKKMMMKPSCSWCK CCCEEEECCCCHHCC	18.84	26051181
85	Ubiquitination	KPSCSWCKDYEQFEE CCCCHHCCCHHHHHH	58.02	29967540
94	Ubiquitination	YEQFEENKQLSILVN HHHHHHHHHHHHHHH	56.76	29967540
104	Acetylation	SILVNCYKKLCEYIT HHHHHHHHHHHHHHH	41.28	7692255
105	Ubiquitination	ILVNCYKKLCEYITQ HHHHHHHHHHHHHHH	31.71	-
109	Phosphorylation	CYKKLCEYITQTTLA HHHHHHHHHHHHHHH	14.31	24719451
113	Phosphorylation	LCEYITQTTLARDII HHHHHHHHHHHHHHH	18.35	24719451
114	Phosphorylation	CEYITQTTLARDIIE HHHHHHHHHHHHHHH	14.49	-
137	Phosphorylation	LALLNDGSLFCEETE HHHHCCCCCEEEECC	22.57	32142685
149	Phosphorylation	ETEKPSDSSFTLCLT ECCCCCCCCEEEEEE	31.52	26074081
150	Phosphorylation	TEKPSDSSFTLCLTH CCCCCCCCEEEEEEC	27.52	26074081
152	Phosphorylation	KPSDSSFTLCLTHSP CCCCCCEEEEEECCC	20.64	26074081
156	Phosphorylation	SSFTLCLTHSPLPST CCEEEEEECCCCCCC	21.22	26074081
158	Phosphorylation	FTLCLTHSPLPSTSE EEEEEECCCCCCCCC	23.93	26074081
162	Phosphorylation	LTHSPLPSTSEPTTD EECCCCCCCCCCCCC	52.85	26074081
163	Phosphorylation	THSPLPSTSEPTTDP ECCCCCCCCCCCCCC	34.86	26074081
164	Phosphorylation	HSPLPSTSEPTTDPQ CCCCCCCCCCCCCCC	46.01	26074081
211	Phosphorylation	RFGINIPSPEHSNTI CCCCCCCCCCCCCCC	38.84	30266825
215	Phosphorylation	NIPSPEHSNTIDVCN CCCCCCCCCCCEECC	33.72	30266825
217	Phosphorylation	PSPEHSNTIDVCNTV CCCCCCCCCEECCCE	22.90	30266825
223	Phosphorylation	NTIDVCNTVDIKTED CCCEECCCEECCHHH	17.90	28450419
228	Phosphorylation	CNTVDIKTEDLSDSL CCCEECCHHHHHCCC	34.76	28270605
261	Ubiquitination	CSFSEDIKPGDSLLL ECCCCCCCCCCEEEE	56.10	-
277	Ubiquitination	VEEVLRSLETVSNTE HHHHHHHCCCCCCCE	5.31	29967540
301	Ubiquitination	LEATVSNGPFLQLSS CEEEECCCCCEEEEC	13.56	29967540
325	Ubiquitination	STSPALHGLSCTAAT CCCHHHHCCCCCCCC	21.82	29967540
335	Ubiquitination	CTAATPKIAKLNRKR CCCCCHHHHHHHHHC	4.26	30230243
343	Phosphorylation	AKLNRKRSRSESDSE HHHHHHCCCCCCCCC	43.10	23401153
345	Phosphorylation	LNRKRSRSESDSEKV HHHHCCCCCCCCCCC	42.57	30266825
347	Phosphorylation	RKRSRSESDSEKVQP HHCCCCCCCCCCCCC	47.92	30266825
349	Phosphorylation	RSRSESDSEKVQPLP CCCCCCCCCCCCCCC	48.90	30266825
351	Ubiquitination	RSESDSEKVQPLPIS CCCCCCCCCCCCCCE	50.55	29967540
358	Phosphorylation	KVQPLPISTIIRGPT CCCCCCCEEEEECCC	16.18	23927012
359	Phosphorylation	VQPLPISTIIRGPTL CCCCCCEEEEECCCC	22.57	23927012
363	Ubiquitination	PISTIIRGPTLGASA CCEEEEECCCCCCCC	14.77	29967540
365	Phosphorylation	STIIRGPTLGASAPV EEEEECCCCCCCCCE	40.42	23312004
369	Phosphorylation	RGPTLGASAPVTVKR ECCCCCCCCCEEEEC	31.16	25159151
373	Phosphorylation	LGASAPVTVKRESKI CCCCCCEEEECCCCC	21.17	32142685
375	Ubiquitination	ASAPVTVKRESKISL CCCCEEEECCCCCCE	40.87	29967540
375	Acetylation	ASAPVTVKRESKISL CCCCEEEECCCCCCE	40.87	25953088
375	Sumoylation	ASAPVTVKRESKISL CCCCEEEECCCCCCE	40.87	28112733
375	Sumoylation	ASAPVTVKRESKISL CCCCEEEECCCCCCE	40.87	-
376	Ubiquitination	SAPVTVKRESKISLQ CCCEEEECCCCCCEE	49.43	29967540
379	Ubiquitination	VTVKRESKISLQPIA EEEECCCCCCEEEEE	31.40	-
380	Ubiquitination	TVKRESKISLQPIAT EEECCCCCCEEEEEE	7.47	29967540
387	Phosphorylation	ISLQPIATVPNGGTT CCEEEEEECCCCCCC	36.90	28122231
393	Phosphorylation	ATVPNGGTTPKISKT EECCCCCCCCCCCEE	41.12	25159151
394	Phosphorylation	TVPNGGTTPKISKTV ECCCCCCCCCCCEEE	26.34	25159151
399	Ubiquitination	GTTPKISKTVLLSTK CCCCCCCEEEEECCC	46.24	29967540
400	Phosphorylation	TTPKISKTVLLSTKS CCCCCCEEEEECCCC	15.03	-
404	Phosphorylation	ISKTVLLSTKSMKKS CCEEEEECCCCCHHH	29.63	24719451
406	Acetylation	KTVLLSTKSMKKSHE EEEEECCCCCHHHHC	45.22	25953088
406	Ubiquitination	KTVLLSTKSMKKSHE EEEEECCCCCHHHHC	45.22	-
409	Ubiquitination	LLSTKSMKKSHEHGS EECCCCCHHHHCCCC	59.21	30230243
419	Phosphorylation	HEHGSKKSHSKTKPG HCCCCCCCCCCCCCC	36.41	-
421	Phosphorylation	HGSKKSHSKTKPGIL CCCCCCCCCCCCCCC	49.46	-
435	Ubiquitination	LKKDKAVKEKIPSHH CCCCHHHHHHCCCCC	59.14	29967540
437	Ubiquitination	KDKAVKEKIPSHHFM CCHHHHHHCCCCCCC	54.95	29967540
440	Phosphorylation	AVKEKIPSHHFMPGS HHHHHCCCCCCCCCC	32.82	29255136
447	Phosphorylation	SHHFMPGSPTKTVYK CCCCCCCCCCCCEEC	24.43	23401153
449	Phosphorylation	HFMPGSPTKTVYKKP CCCCCCCCCCEECCC	40.83	29255136
450	Ubiquitination	FMPGSPTKTVYKKPQ CCCCCCCCCEECCCC	39.10	29967540
453	Phosphorylation	GSPTKTVYKKPQEKK CCCCCCEECCCCCCC	20.65	17053785
454	Ubiquitination	SPTKTVYKKPQEKKG CCCCCEECCCCCCCC	54.35	29967540
488	Ubiquitination	CPCYSNRKACLDCIC CCCCCCCCHHHHHHH	47.94	-
501	Phosphorylation	ICRGCQNSYMANGEK HHHCCCCCHHCCCCH	7.15	29978859
502	Phosphorylation	CRGCQNSYMANGEKK HHCCCCCHHCCCCHH	14.06	29978859
508	Acetylation	SYMANGEKKLEAFAV CHHCCCCHHEEEEEC	65.15	26051181
508	Ubiquitination	SYMANGEKKLEAFAV CHHCCCCHHEEEEEC	65.15	-
509	Ubiquitination	YMANGEKKLEAFAVP HHCCCCHHEEEEECC	47.46	29967540
509	Acetylation	YMANGEKKLEAFAVP HHCCCCHHEEEEECC	47.46	26051181
518	Ubiquitination	EAFAVPEKALEQTRL EEEECCHHHHHHHHE	52.80	-
518	Acetylation	EAFAVPEKALEQTRL EEEECCHHHHHHHHE	52.80	25953088
540	Phosphorylation	SIAVRNASTSTSVIN EEEEEECCCCCEEEE	26.83	30108239
541	Phosphorylation	IAVRNASTSTSVINV EEEEECCCCCEEEEC	33.35	27251275
542	Phosphorylation	AVRNASTSTSVINVT EEEECCCCCEEEECC	19.05	27251275
543	Phosphorylation	VRNASTSTSVINVTG EEECCCCCEEEECCC	27.40	27251275
544	Phosphorylation	RNASTSTSVINVTGS EECCCCCEEEECCCC	22.29	30108239
549	Phosphorylation	STSVINVTGSPVTTF CCEEEECCCCCCCEE	27.70	28450419
551	Phosphorylation	SVINVTGSPVTTFLA EEEECCCCCCCEEEE	13.56	28450419
554	Phosphorylation	NVTGSPVTTFLAAST ECCCCCCCEEEECCC	18.40	28450419
555	Phosphorylation	VTGSPVTTFLAASTH CCCCCCCEEEECCCC	19.52	28450419
560	Phosphorylation	VTTFLAASTHDDKSL CCEEEECCCCCCCCH	22.22	22199227
561	Phosphorylation	TTFLAASTHDDKSLD CEEEECCCCCCCCHH	25.29	-
566	Phosphorylation	ASTHDDKSLDEAIDM CCCCCCCCHHHHHHH	48.31	25849741

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 MSL2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MSL2_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 MSL2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
P53_HUMAN	TP53	physical	19033443
H2A2C_HUMAN	HIST2H2AC	physical	21726816
H2A2A_HUMAN	HIST2H2AA3	physical	21726816
H2B2E_HUMAN	HIST2H2BE	physical	21726816
H32_HUMAN	HIST2H3C	physical	21726816
UB2D3_HUMAN	UBE2D3	physical	21726816
TRIM8_HUMAN	TRIM8	physical	22493164
H2B2E_HUMAN	HIST2H2BE	physical	24837678
UB2D3_HUMAN	UBE2D3	physical	24837678
BRE1A_HUMAN	RNF20	physical	24837678
BRE1B_HUMAN	RNF40	physical	24837678
PAF1_HUMAN	PAF1	physical	24837678
CDK9_HUMAN	CDK9	physical	24837678
MSL1_HUMAN	MSL1	physical	28514442
KAT8_HUMAN	KAT8	physical	28514442
MS3L1_HUMAN	MSL3	physical	28514442
HBB_HUMAN	HBB	physical	28514442

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 MSL2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling."; Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.; EMBO J. 25:5058-5070(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-453, AND MASSSPECTROMETRY.	17053785 [Abstract]