dbPTM

MO4L2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MO4L2_HUMAN
UniProt AC	Q15014
Protein Name	Mortality factor 4-like protein 2
Gene Name	MORF4L2
Organism	Homo sapiens (Human).
Sequence Length	288
Subcellular Localization	Nucleus.
Protein Description	Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Also component of the MSIN3A complex which acts to repress transcription by deacetylation of nucleosomal histones..
Protein Sequence	MSSRKQGSQPRGQQSAEEENFKKPTRSNMQRSKMRGASSGKKTAGPQQKNLEPALPGRWGGRSAENPPSGSVRKTRKNKQKTPGNGDGGSTSEAPQPPRKKRARADPTVESEEAFKNRMEVKVKIPEELKPWLVEDWDLVTRQKQLFQLPAKKNVDAILEEYANCKKSQGNVDNKEYAVNEVVAGIKEYFNVMLGTQLLYKFERPQYAEILLAHPDAPMSQVYGAPHLLRLFVRIGAMLAYTPLDEKSLALLLGYLHDFLKYLAKNSASLFTASDYKVASAEYHRKAL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSRKQGSQ ------CCCCCCCCC	38.56	-
3	Phosphorylation	-----MSSRKQGSQP -----CCCCCCCCCC	42.05	-
4	Methylation	----MSSRKQGSQPR ----CCCCCCCCCCC	28.19	24384445
8	O-linked_Glycosylation	MSSRKQGSQPRGQQS CCCCCCCCCCCCCCC	34.22	30379171
11	Methylation	RKQGSQPRGQQSAEE CCCCCCCCCCCCHHH	48.17	24384453
15	Phosphorylation	SQPRGQQSAEEENFK CCCCCCCCHHHHHCC	29.75	21815630
22	Methylation	SAEEENFKKPTRSNM CHHHHHCCCCCHHHH	70.22	115973195
22	Ubiquitination	SAEEENFKKPTRSNM CHHHHHCCCCCHHHH	70.22	33845483
23	Acetylation	AEEENFKKPTRSNMQ HHHHHCCCCCHHHHH	47.70	23749302
23	Ubiquitination	AEEENFKKPTRSNMQ HHHHHCCCCCHHHHH	47.70	29967540
25	Phosphorylation	EENFKKPTRSNMQRS HHHCCCCCHHHHHHH	56.46	19413330
35	Methylation	NMQRSKMRGASSGKK HHHHHHHCCCCCCCC	41.06	54557401
42	Ubiquitination	RGASSGKKTAGPQQK CCCCCCCCCCCCCCC	47.32	24816145
49	Ubiquitination	KTAGPQQKNLEPALP CCCCCCCCCCCCCCC	59.25	27667366
63	Phosphorylation	PGRWGGRSAENPPSG CCCCCCCCCCCCCCC	43.12	26329039
69	Phosphorylation	RSAENPPSGSVRKTR CCCCCCCCCCCCCCC	44.98	23401153
71	Phosphorylation	AENPPSGSVRKTRKN CCCCCCCCCCCCCCC	24.08	23401153
75	Phosphorylation	PSGSVRKTRKNKQKT CCCCCCCCCCCCCCC	35.99	28111955
81	Ubiquitination	KTRKNKQKTPGNGDG CCCCCCCCCCCCCCC	59.29	24816145
82	Phosphorylation	TRKNKQKTPGNGDGG CCCCCCCCCCCCCCC	33.65	21815630
90	Phosphorylation	PGNGDGGSTSEAPQP CCCCCCCCCCCCCCC	34.00	25159151
91	Phosphorylation	GNGDGGSTSEAPQPP CCCCCCCCCCCCCCC	33.58	22210691
92	Phosphorylation	NGDGGSTSEAPQPPR CCCCCCCCCCCCCCC	33.20	28555341
100	Ubiquitination	EAPQPPRKKRARADP CCCCCCCCCCCCCCC	53.00	29967540
101	Ubiquitination	APQPPRKKRARADPT CCCCCCCCCCCCCCC	53.20	29967540
116	Ubiquitination	VESEEAFKNRMEVKV CCCHHHHHHCCEEEE	51.17	33845483
124	Ubiquitination	NRMEVKVKIPEELKP HCCEEEEECCHHHHH	46.99	33845483
130	Ubiquitination	VKIPEELKPWLVEDW EECCHHHHHHHHCCC	37.11	29967540
144	Ubiquitination	WDLVTRQKQLFQLPA CCHHHHHHHHHCCCC	45.75	29967540
152	Ubiquitination	QLFQLPAKKNVDAIL HHHCCCCCCCHHHHH	42.83	29967540
153	Ubiquitination	LFQLPAKKNVDAILE HHCCCCCCCHHHHHH	65.39	29967540
166	Ubiquitination	LEEYANCKKSQGNVD HHHHHCCCHHHCCCC	56.09	32015554
167	Ubiquitination	EEYANCKKSQGNVDN HHHHCCCHHHCCCCC	50.65	29967540
175	Ubiquitination	SQGNVDNKEYAVNEV HHCCCCCHHHHHHHH	47.87	32015554
238	Sulfoxidation	LFVRIGAMLAYTPLD HHHHHHCHHHCCCCC	1.53	28183972
241	Phosphorylation	RIGAMLAYTPLDEKS HHHCHHHCCCCCHHH	12.62	19835603
242	Phosphorylation	IGAMLAYTPLDEKSL HHCHHHCCCCCHHHH	16.27	19835603
262	Phosphorylation	YLHDFLKYLAKNSAS HHHHHHHHHHHCCCC	17.65	19835603
265	Ubiquitination	DFLKYLAKNSASLFT HHHHHHHHCCCCCCC	49.17	33845483
267	Phosphorylation	LKYLAKNSASLFTAS HHHHHHCCCCCCCCC	20.66	21082442
276	Phosphorylation	SLFTASDYKVASAEY CCCCCCHHHHCCHHH	12.60	22817900
277	Ubiquitination	LFTASDYKVASAEYH CCCCCHHHHCCHHHH	35.99	22053931
283	Phosphorylation	YKVASAEYHRKAL-- HHHCCHHHHHHCC--	13.47	18083107
286	Ubiquitination	ASAEYHRKAL----- CCHHHHHHCC-----	40.50	29967540

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 MO4L2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MO4L2_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 MO4L2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RB_HUMAN	RB1	physical	14506250
MOFA1_HUMAN	MRFAP1	physical	14506250
HDAC9_HUMAN	HDAC9	physical	14506250
SIN3A_HUMAN	SIN3A	physical	12391155
SRCAP_HUMAN	SRCAP	physical	17573780
KDM5A_HUMAN	KDM5A	physical	17573780
BRD8_HUMAN	BRD8	physical	17573780
SIN3B_HUMAN	SIN3B	physical	17573780
PHF12_HUMAN	PHF12	physical	17573780
EPC1_HUMAN	EPC1	physical	17573780
EPC2_HUMAN	EPC2	physical	17573780
IMB1_HUMAN	KPNB1	physical	17573780
HNRPU_HUMAN	HNRNPU	physical	17573780
ZN131_HUMAN	ZNF131	physical	17573780
MBTD1_HUMAN	MBTD1	physical	17573780
HSP74_HUMAN	HSPA4	physical	17573780
HNRPM_HUMAN	HNRNPM	physical	17573780
LMNA_HUMAN	LMNA	physical	17573780
HDAC1_HUMAN	HDAC1	physical	17573780
HDAC2_HUMAN	HDAC2	physical	17573780
DMAP1_HUMAN	DMAP1	physical	17573780
HNRPK_HUMAN	HNRNPK	physical	17573780
TBB2A_HUMAN	TUBB2A	physical	17573780
TBA1A_HUMAN	TUBA1A	physical	17573780
IMA1_HUMAN	KPNA2	physical	17573780
KAT5_HUMAN	KAT5	physical	17573780
RBBP7_HUMAN	RBBP7	physical	17573780
RUVB1_HUMAN	RUVBL1	physical	17573780
RUVB2_HUMAN	RUVBL2	physical	17573780
ACL6A_HUMAN	ACTL6A	physical	17573780
ACTS_HUMAN	ACTA1	physical	17573780
ACTB_HUMAN	ACTB	physical	17573780
ACTG_HUMAN	ACTG1	physical	17573780
MRGBP_HUMAN	MRGBP	physical	17573780
MOFA1_HUMAN	MRFAP1	physical	17573780
H2AV_HUMAN	H2AFV	physical	17573780
H2B2E_HUMAN	HIST2H2BE	physical	17573780
PALB2_HUMAN	PALB2	physical	20332121
TRRAP_HUMAN	TRRAP	physical	20332121
EP400_HUMAN	EP400	physical	20332121
RET2_HUMAN	RBP2	physical	20332121
BRD8_HUMAN	BRD8	physical	20332121
SIN3B_HUMAN	SIN3B	physical	20332121
PHF12_HUMAN	PHF12	physical	20332121
EPC1_HUMAN	EPC1	physical	20332121
EPC2_HUMAN	EPC2	physical	20332121
HDAC1_HUMAN	HDAC1	physical	20332121
HDAC2_HUMAN	HDAC2	physical	20332121
KAT5_HUMAN	KAT5	physical	20332121
RBBP7_HUMAN	RBBP7	physical	20332121
RUVB1_HUMAN	RUVBL1	physical	20332121
RUVB2_HUMAN	RUVBL2	physical	20332121
MRGBP_HUMAN	MRGBP	physical	20332121
H2A2C_HUMAN	HIST2H2AC	physical	20332121
H2B2E_HUMAN	HIST2H2BE	physical	20332121
CDR2_HUMAN	CDR2	physical	11988016
TNIP1_HUMAN	TNIP1	physical	25416956
IKZF1_HUMAN	IKZF1	physical	25416956
PNMA2_HUMAN	PNMA2	physical	25416956
ZBT43_HUMAN	ZBTB43	physical	25416956
KLHL3_HUMAN	KLHL3	physical	25416956
ZBT7B_HUMAN	ZBTB7B	physical	25416956
THAP1_HUMAN	THAP1	physical	25416956
CEP55_HUMAN	CEP55	physical	25416956
MRGBP_HUMAN	MRGBP	physical	25416956
GRM2B_HUMAN	GRAMD3	physical	25416956
ZBT10_HUMAN	ZBTB10	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
LMBL3_HUMAN	L3MBTL3	physical	25416956
MOFA1_HUMAN	MRFAP1	physical	25416956
MR1L1_HUMAN	MRFAP1L1	physical	25416956
DDT4L_HUMAN	DDIT4L	physical	25416956
FAM9B_HUMAN	FAM9B	physical	25416956
BEND7_HUMAN	BEND7	physical	25416956
HDAC2_HUMAN	HDAC2	physical	26344197
MRGBP_HUMAN	MRGBP	physical	26344197
TRRAP_HUMAN	TRRAP	physical	26344197
VAPB_HUMAN	VAPB	physical	26344197
MR1L1_HUMAN	MRFAP1L1	physical	28514442
PALB2_HUMAN	PALB2	physical	28514442
BRD8_HUMAN	BRD8	physical	28514442
ASH1L_HUMAN	ASH1L	physical	28514442
EP400_HUMAN	EP400	physical	28514442
PHF12_HUMAN	PHF12	physical	28514442
SATB2_HUMAN	SATB2	physical	28514442
EPC1_HUMAN	EPC1	physical	28514442
MBTD1_HUMAN	MBTD1	physical	28514442
EPC2_HUMAN	EPC2	physical	28514442
MOFA1_HUMAN	MRFAP1	physical	28514442
TRRAP_HUMAN	TRRAP	physical	28514442
KAT5_HUMAN	KAT5	physical	28514442
VPS72_HUMAN	VPS72	physical	28514442
ING3_HUMAN	ING3	physical	28514442
DMAP1_HUMAN	DMAP1	physical	28514442
JAZF1_HUMAN	JAZF1	physical	28514442
YETS4_HUMAN	YEATS4	physical	28514442
BRCA2_HUMAN	BRCA2	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 MO4L2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-71, AND MASSSPECTROMETRY.	18669648 [Abstract]