MAD1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MAD1_HUMAN
• UniProt AC: Q05195
• Protein Name: Max dimerization protein 1
• Gene Name: MXD1
• Organism: Homo sapiens (Human).
• Sequence Length: 221
• Subcellular Localization: Nucleus.
• Protein Description: Transcriptional repressor. MAD binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. MAD thus antagonizes MYC transcriptional activity by competing for MAX..
• Protein Sequence: MAAAVRMNIQMLLEAADYLERREREAEHGYASMLPYNNKDRDALKRRNKSKKNNSSSRSTHNEMEKNRRAHLRLCLEKLKGLVPLGPESSRHTTLSLLTKAKLHIKKLEDCDRKAVHQIDQLQREQRHLKRQLEKLGIERIRMDSIGSTVSSERSDSDREEIDVDVESTDYLTGDLDWSSSSVSDSDERGSMQSLGSDEGYSSTSIKRIKLQDSHKACLGL

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
30	Phosphorylation	EREAEHGYASMLPYN HHHHHHCCCCCCCCC	9.45	27067055
32	Phosphorylation	EAEHGYASMLPYNNK HHHHCCCCCCCCCCC	16.62	27067055
36	Phosphorylation	GYASMLPYNNKDRDA CCCCCCCCCCCCHHH	27.66	27067055
39	Acetylation	SMLPYNNKDRDALKR CCCCCCCCCHHHHHH	50.97	19811681
55 (in isoform 2)	Phosphorylation	-	38.80	22210691
89	Phosphorylation	LVPLGPESSRHTTLS CCCCCCCCCCHHHHH	35.49	26330541
90	Phosphorylation	VPLGPESSRHTTLSL CCCCCCCCCHHHHHH	26.81	26330541
93	Phosphorylation	GPESSRHTTLSLLTK CCCCCCHHHHHHHHH	28.46	23911959
94	Phosphorylation	PESSRHTTLSLLTKA CCCCCHHHHHHHHHH	14.28	23911959
96	Phosphorylation	SSRHTTLSLLTKAKL CCCHHHHHHHHHHHH	21.17	24719451
99	Phosphorylation	HTTLSLLTKAKLHIK HHHHHHHHHHHHHHH	33.96	30622161
100	Ubiquitination	TTLSLLTKAKLHIKK HHHHHHHHHHHHHHC	43.42	-
114	Ubiquitination	KLEDCDRKAVHQIDQ CHHHCCHHHHHHHHH	41.32	-
135	Ubiquitination	HLKRQLEKLGIERIR HHHHHHHHHCCCEEE	61.68	-
145	Phosphorylation	IERIRMDSIGSTVSS CCEEEECCCCCCCCC	21.36	22817900
189	Methylation	SVSDSDERGSMQSLG CCCCCCCCCCCHHCC	47.69	115386205
191	Phosphorylation	SDSDERGSMQSLGSD CCCCCCCCCHHCCCC	21.62	23663014
194	Phosphorylation	DERGSMQSLGSDEGY CCCCCCHHCCCCCCC	26.51	23663014
197	Phosphorylation	GSMQSLGSDEGYSST CCCHHCCCCCCCCCC	37.47	23663014
201	Phosphorylation	SLGSDEGYSSTSIKR HCCCCCCCCCCCEEE	9.44	23663014
202	Phosphorylation	LGSDEGYSSTSIKRI CCCCCCCCCCCEEEE	37.69	23663014
203	Phosphorylation	GSDEGYSSTSIKRIK CCCCCCCCCCEEEEE	20.07	23663014
204	Phosphorylation	SDEGYSSTSIKRIKL CCCCCCCCCEEEEEE	28.65	23663014
205	Phosphorylation	DEGYSSTSIKRIKLQ CCCCCCCCEEEEEEC	28.23	23663014

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
145	S	Phosphorylation	Kinase	AKT1	P31749	PSP
145	S	Phosphorylation	Kinase	RPS6KA1	Q15418	GPS
145	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
145	S	Phosphorylation	Kinase	RPS6KB1	P23443	GPS
145	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	BIRC2	Q13490	PMID:18082613

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MAD1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of MAD1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MAX_HUMAN	MAX	physical	8425218
SIN3A_HUMAN	SIN3A	physical	7889570
SIN3B_MOUSE	Sin3b	physical	11101889
SIN3A_MOUSE	Sin3a	physical	11101889
SAP30_HUMAN	SAP30	physical	11101889
HDAC1_HUMAN	HDAC1	physical	11101889
HDAC2_HUMAN	HDAC2	physical	11101889
MLX_HUMAN	MLX	physical	11230181
KDM5A_HUMAN	KDM5A	physical	19762557
AKT1_HUMAN	AKT1	physical	19526459
MAX_HUMAN	MAX	physical	17418410
BIRC2_HUMAN	BIRC2	physical	18082613
A4_HUMAN	APP	physical	21832049
VDR_HUMAN	VDR	physical	23112173
SIN3A_HUMAN	SIN3A	physical	26186194
SP130_HUMAN	SAP130	physical	26186194
BRM1L_HUMAN	BRMS1L	physical	26186194
SP30L_HUMAN	SAP30L	physical	26186194
MAX_HUMAN	MAX	physical	26186194
ARI4B_HUMAN	ARID4B	physical	26186194
SDS3_HUMAN	SUDS3	physical	26186194
ARI4A_HUMAN	ARID4A	physical	26186194
BRMS1_HUMAN	BRMS1	physical	26186194
ARI4B_HUMAN	ARID4B	physical	28514442
SP130_HUMAN	SAP130	physical	28514442
SDS3_HUMAN	SUDS3	physical	28514442
SIN3A_HUMAN	SIN3A	physical	28514442
MAX_HUMAN	MAX	physical	28514442
BRMS1_HUMAN	BRMS1	physical	28514442
ARI4A_HUMAN	ARID4A	physical	28514442
BRM1L_HUMAN	BRMS1L	physical	28514442
SP30L_HUMAN	SAP30L	physical	28514442
E2F6_HUMAN	E2F6	physical	29028833
TFDP1_HUMAN	TFDP1	physical	29028833
MGAP_HUMAN	MGA	physical	29028833
PCGF6_HUMAN	PCGF6	physical	29028833
RING1_HUMAN	RING1	physical	29028833
CBX3_HUMAN	CBX3	physical	29028833
RING2_HUMAN	RNF2	physical	29028833
LMBL2_HUMAN	L3MBTL2	physical	29028833
RYBP_HUMAN	RYBP	physical	29028833
YAF2_HUMAN	YAF2	physical	29028833
MAD3_HUMAN	MXD3	physical	29028833
MAD4_HUMAN	MXD4	physical	29028833
MNT_HUMAN	MNT	physical	29028833
SIN3A_HUMAN	SIN3A	physical	29028833

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.