dbPTM

MAX_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MAX_HUMAN
UniProt AC	P61244
Protein Name	Protein max {ECO:0000305}
Gene Name	MAX {ECO:0000312\|HGNC:HGNC:6913}
Organism	Homo sapiens (Human).
Sequence Length	160
Subcellular Localization	Nucleus. Cell projection, dendrite.
Protein Description	Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional activator, whereas the MAD:MAX complex is a repressor. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity. Represses MYC transcriptional activity from E-box elements..
Protein Sequence	MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSDNDDIEV ------CCCCCCCCC	45.16	28355574
2	Acetylation	------MSDNDDIEV ------CCCCCCCCC	45.16	19413330
2 (in isoform 2)	Acetylation	-	45.16	21406692
2 (in isoform 2)	Phosphorylation	-	45.16	28355574
11	Phosphorylation	NDDIEVESDEEQPRF CCCCCCCCCCCCHHH	56.34	29255136
11 (in isoform 2)	Phosphorylation	-	56.34	22167270
20	Phosphorylation	EEQPRFQSAADKRAH CCCHHHHHHHHHHHH	23.78	27486199
24	Acetylation	RFQSAADKRAHHNAL HHHHHHHHHHHHHHH	46.92	25953088
24	Ubiquitination	RFQSAADKRAHHNAL HHHHHHHHHHHHHHH	46.92	-
40	Acetylation	RKRRDHIKDSFHSLR HHHHHHHHHHHHHHH	43.85	26051181
40	Ubiquitination	RKRRDHIKDSFHSLR HHHHHHHHHHHHHHH	43.85	-
42	Phosphorylation	RRDHIKDSFHSLRDS HHHHHHHHHHHHHHC	21.62	24532841
45	Phosphorylation	HIKDSFHSLRDSVPS HHHHHHHHHHHCCHH	24.08	28555341
49	Phosphorylation	SFHSLRDSVPSLQGE HHHHHHHCCHHHCCC	29.50	7479834
57	Ubiquitination	VPSLQGEKASRAQIL CHHHCCCHHHHHHHH	59.49	-
66	Acetylation	SRAQILDKATEYIQY HHHHHHHHHHHHHHH	54.48	17217336
68	Phosphorylation	AQILDKATEYIQYMR HHHHHHHHHHHHHHH	34.75	-
70	Phosphorylation	ILDKATEYIQYMRRK HHHHHHHHHHHHHHC	6.75	22817900
73	Phosphorylation	KATEYIQYMRRKNHT HHHHHHHHHHHCCCC	5.30	23532336
75	Methylation	TEYIQYMRRKNHTHQ HHHHHHHHHCCCCCC	41.30	115482711
89	Methylation	QQDIDDLKRQNALLE CCCHHHHHHHHHHHH	59.96	115972851
89	Ubiquitination	QQDIDDLKRQNALLE CCCHHHHHHHHHHHH	59.96	-
107	Phosphorylation	RALEKARSSAQLQTN HHHHHHHHHHHHCCC	34.58	30576142
108	Phosphorylation	ALEKARSSAQLQTNY HHHHHHHHHHHCCCC	17.93	30576142
115	Phosphorylation	SAQLQTNYPSSDNSL HHHHCCCCCCCCCCC	14.10	22817900
117	Phosphorylation	QLQTNYPSSDNSLYT HHCCCCCCCCCCCEE	39.71	29978859
118	Phosphorylation	LQTNYPSSDNSLYTN HCCCCCCCCCCCEEC	35.99	25159151
121	Phosphorylation	NYPSSDNSLYTNAKG CCCCCCCCCEECCCC	27.95	28796482
123	Phosphorylation	PSSDNSLYTNAKGST CCCCCCCEECCCCCE	9.58	28796482
124	Phosphorylation	SSDNSLYTNAKGSTI CCCCCCEECCCCCEE	33.71	28796482
129	Phosphorylation	LYTNAKGSTISAFDG CEECCCCCEEEECCC	23.12	26552605
130	Phosphorylation	YTNAKGSTISAFDGG EECCCCCEEEECCCC	27.85	26552605
132	Phosphorylation	NAKGSTISAFDGGSD CCCCCEEEECCCCCC	23.99	26552605
138	Phosphorylation	ISAFDGGSDSSSESE EEECCCCCCCCCCCC	39.59	20363803
140	Phosphorylation	AFDGGSDSSSESEPE ECCCCCCCCCCCCCC	37.14	17081983
141	Phosphorylation	FDGGSDSSSESEPEE CCCCCCCCCCCCCCC	43.02	17081983
142	Phosphorylation	DGGSDSSSESEPEEP CCCCCCCCCCCCCCC	49.44	25137130
144	Phosphorylation	GSDSSSESEPEEPQS CCCCCCCCCCCCCHH	61.47	28355574
151	Phosphorylation	SEPEEPQSRKKLRME CCCCCCHHHHHHHHH	57.70	27251275
153	Acetylation	PEEPQSRKKLRMEAS CCCCHHHHHHHHHCC	62.50	17217336
154	Acetylation	EEPQSRKKLRMEAS- CCCHHHHHHHHHCC-	39.97	17217336

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
2	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
2	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
2	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
11	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
11	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
11	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PKHF2_HUMAN	PLEKHF2	physical	16189514
MXI1_HUMAN	MXI1	physical	16189514
MYC_HUMAN	MYC	physical	10611234
KAT2A_HUMAN	KAT2A	physical	10611234
TRRAP_HUMAN	TRRAP	physical	10611234
MYC_HUMAN	MYC	physical	9708738
TRRAP_HUMAN	TRRAP	physical	9708738
EP400_HUMAN	EP400	physical	11509179
MSH2_HUMAN	MSH2	physical	12584560
MYC_HUMAN	MYC	physical	12584560
JIP4_HUMAN	SPAG9	physical	12391307
MYC_HUMAN	MYC	physical	12391307
MAD1_HUMAN	MXD1	physical	12391307
MAD3_HUMAN	MXD3	physical	9528857
MAD4_HUMAN	MXD4	physical	9528857
MYC_HUMAN	MYC	physical	9528857
MAD1_HUMAN	MXD1	physical	9528857
MNT_HUMAN	MNT	physical	9184233
MXI1_HUMAN	MXI1	physical	9184233
MAD3_HUMAN	MXD3	physical	9184233
MYC_HUMAN	MYC	physical	9184233
MAX_HUMAN	MAX	physical	12553908
MYC_HUMAN	MYC	physical	12553908
MAD1_HUMAN	MXD1	physical	12553908
MAX_HUMAN	MAX	physical	9115440
MYC_HUMAN	MYC	physical	10229200
MYCN_HUMAN	MYCN	physical	10229200
MYCL_HUMAN	MYCL	physical	10229200
MXI1_HUMAN	MXI1	physical	10229200
MAD3_HUMAN	MXD3	physical	10229200
MAD4_HUMAN	MXD4	physical	10229200
MYC_HUMAN	MYC	physical	10918583
MAD3_HUMAN	MXD3	physical	10918583
MAX_HUMAN	MAX	physical	17217336
MYC_HUMAN	MYC	physical	16140957
MAD1_HUMAN	MXD1	physical	16140957
CUX1_HUMAN	CUX1	physical	20936779
CASP_HUMAN	CUX1	physical	20936779
MYC_HUMAN	MYC	physical	20936779
TAF1_HUMAN	TAF1	physical	20936779
CLIP2_HUMAN	CLIP2	physical	20936779
CSN5_HUMAN	COPS5	physical	20936779
MGAP_HUMAN	MGA	physical	20936779
PKHA5_HUMAN	PLEKHA5	physical	20936779
TXLNG_HUMAN	TXLNG	physical	20936779
CEBPA_HUMAN	CEBPA	physical	17082780
TYY1_HUMAN	YY1	physical	16878156
MYC_HUMAN	MYC	physical	16596619
MAD1_HUMAN	MXD1	physical	16596619
EP300_HUMAN	EP300	physical	16287840
MYC_HUMAN	MYC	physical	12824180
MXI1_HUMAN	MXI1	physical	15467743
MYC_HUMAN	MYC	physical	17418410
HIF1A_HUMAN	HIF1A	physical	17418410
EPAS1_HUMAN	EPAS1	physical	17418410
PIM1_HUMAN	PIM1	physical	17643117
MYC_HUMAN	MYC	physical	17643117
TRRAP_HUMAN	TRRAP	physical	20946988
MNT_HUMAN	MNT	physical	20946988
EP400_HUMAN	EP400	physical	20946988
DMAP1_HUMAN	DMAP1	physical	20946988
MYCN_HUMAN	MYCN	physical	20946988
WDR5_HUMAN	WDR5	physical	20946988
MYC_HUMAN	MYC	physical	20946988
KAT5_HUMAN	KAT5	physical	20946988
BRD8_HUMAN	BRD8	physical	20946988
MXI1_HUMAN	MXI1	physical	20946988
PCGF6_HUMAN	PCGF6	physical	20946988
MAX_HUMAN	MAX	physical	20946988
PRAF3_HUMAN	ARL6IP5	physical	22939629
KMT2D_HUMAN	KMT2D	physical	22939629
MAD1_HUMAN	MXD1	physical	8224841
MYC_HUMAN	MYC	physical	8224841
MYC_HUMAN	MYC	physical	14749374
MYC_HUMAN	MYC	physical	10465786
MAD1_HUMAN	MXD1	physical	9886493
MYC_HUMAN	MYC	physical	23816886
MYC_HUMAN	MYC	physical	21988832
PLIN3_HUMAN	PLIN3	physical	21988832
MGAP_HUMAN	MGA	physical	21988832
MYC_HUMAN	MYC	physical	19623651
GABR1_HUMAN	GABBR1	physical	20195357
FRIH_HUMAN	FTH1	physical	20195357
RL35_HUMAN	RPL35	physical	20195357
FUS_HUMAN	FUS	physical	20195357
RL34_HUMAN	RPL34	physical	20195357
TBA1A_HUMAN	TUBA1A	physical	20195357
UBP37_HUMAN	USP37	physical	25284584
MXI1_HUMAN	MXI1	physical	25416956
BANP_HUMAN	BANP	physical	25416956
UN45A_HUMAN	UNC45A	physical	25416956
MAX_HUMAN	MAX	physical	9050988
MAD1_HUMAN	MXD1	physical	10229200
MSH2_HUMAN	MSH2	physical	25241761
SMAD3_HUMAN	SMAD3	physical	25241761
MGAP_HUMAN	MGA	physical	25609649
LMBL2_HUMAN	L3MBTL2	physical	25609649
MECP2_HUMAN	MECP2	physical	25609649
SIN3A_HUMAN	SIN3A	physical	25609649
E2F6_HUMAN	E2F6	physical	25609649
RING2_HUMAN	RNF2	physical	25609649
EP400_HUMAN	EP400	physical	25609649
EF1D_HUMAN	EEF1D	physical	25609649
FOXK2_HUMAN	FOXK2	physical	25609649
MORC2_HUMAN	MORC2	physical	25609649
MNT_HUMAN	MNT	physical	25609649
MAD4_HUMAN	MXD4	physical	25609649
PCGF6_HUMAN	PCGF6	physical	25609649
SMCA5_HUMAN	SMARCA5	physical	25609649
DMAP1_HUMAN	DMAP1	physical	25609649
MXI1_HUMAN	MXI1	physical	25609649
MYC_HUMAN	MYC	physical	25609649
RECQ1_HUMAN	RECQL	physical	25609649
SP130_HUMAN	SAP130	physical	25609649
BAZ1A_HUMAN	BAZ1A	physical	25609649
FOXK1_HUMAN	FOXK1	physical	25609649
H2AY_HUMAN	H2AFY	physical	25609649
SMCA1_HUMAN	SMARCA1	physical	25609649
TBP_HUMAN	TBP	physical	25609649
AP2A_HUMAN	TFAP2A	physical	25609649
TFDP1_HUMAN	TFDP1	physical	25609649
TWST1_HUMAN	TWIST1	physical	25609649
WIZ_HUMAN	WIZ	physical	25609649
YETS4_HUMAN	YEATS4	physical	25609649
RFA2_HUMAN	RPA2	physical	25609649
MTEF1_HUMAN	MTERF1	physical	25609649
VRK3_HUMAN	VRK3	physical	25609649
DNLI3_HUMAN	LIG3	physical	25609649
XRCC1_HUMAN	XRCC1	physical	25609649
MYC_HUMAN	MYC	physical	25522242
TCP1L_HUMAN	TCP10L	physical	28514442
CU077_HUMAN	TCP10L	physical	28514442
BMAL1_HUMAN	ARNTL	physical	27173435
RPR1A_HUMAN	RPRD1A	physical	27173435
HAUS6_HUMAN	HAUS6	physical	27173435
PHLB3_HUMAN	PHLDB3	physical	27173435
CAVN1_HUMAN	PTRF	physical	27173435
PF21A_HUMAN	PHF21A	physical	27173435
MS18B_HUMAN	OIP5	physical	27173435
CCD93_HUMAN	CCDC93	physical	27173435
VPS50_HUMAN	CCDC132	physical	27173435
HM20A_HUMAN	HMG20A	physical	27173435
RCOR1_HUMAN	RCOR1	physical	27173435
GRAP1_HUMAN	GRIPAP1	physical	27173435
DZIP3_HUMAN	DZIP3	physical	27173435
VPS53_HUMAN	VPS53	physical	27173435
PSMD9_HUMAN	PSMD9	physical	27173435
CLOCK_HUMAN	CLOCK	physical	27173435
GOGA5_HUMAN	GOLGA5	physical	27173435
RBG10_HUMAN	RABGAP1L	physical	27173435
RBG1L_HUMAN	RABGAP1L	physical	27173435
TUFT1_HUMAN	TUFT1	physical	27173435
YETS4_HUMAN	YEATS4	physical	27173435
CCHCR_HUMAN	CCHCR1	physical	27173435
KDM1A_HUMAN	KDM1A	physical	27173435
TFPT_HUMAN	TFPT	physical	27173435
NCK5L_HUMAN	NCKAP5L	physical	27173435
GIT2_HUMAN	GIT2	physical	27173435
NUF2_HUMAN	NUF2	physical	27173435
THA11_HUMAN	THAP11	physical	27173435
JUN_HUMAN	JUN	physical	27173435
PKN3_HUMAN	PKN3	physical	27173435
RABX5_HUMAN	RABGEF1	physical	27173435
MYCL_HUMAN	MYCL	physical	29028833
MYCN_HUMAN	MYCN	physical	29028833
PP2AA_HUMAN	PPP2CA	physical	29028833
2AAA_HUMAN	PPP2R1A	physical	29028833
2AAB_HUMAN	PPP2R1B	physical	29028833
PP2AB_HUMAN	PPP2CB	physical	29028833
TRRAP_HUMAN	TRRAP	physical	29028833
EP400_HUMAN	EP400	physical	29028833
KAT5_HUMAN	KAT5	physical	29028833
EPC1_HUMAN	EPC1	physical	29028833
EPC2_HUMAN	EPC2	physical	29028833
ING3_HUMAN	ING3	physical	29028833
DMAP1_HUMAN	DMAP1	physical	29028833
RUVB1_HUMAN	RUVBL1	physical	29028833
RUVB2_HUMAN	RUVBL2	physical	29028833
ACL6A_HUMAN	ACTL6A	physical	29028833
ACL6B_HUMAN	ACTL6B	physical	29028833
MO4L1_HUMAN	MORF4L1	physical	29028833
MO4L2_HUMAN	MORF4L2	physical	29028833
EAF6_HUMAN	MEAF6	physical	29028833
MRGBP_HUMAN	MRGBP	physical	29028833
YETS4_HUMAN	YEATS4	physical	29028833
BRD8_HUMAN	BRD8	physical	29028833
VPS72_HUMAN	VPS72	physical	29028833
MBTD1_HUMAN	MBTD1	physical	29028833
MAD1_HUMAN	MXD1	physical	29028833
MAD3_HUMAN	MXD3	physical	29028833
MAD4_HUMAN	MXD4	physical	29028833
MNT_HUMAN	MNT	physical	29028833
SIN3A_HUMAN	SIN3A	physical	29028833
E2F6_HUMAN	E2F6	physical	29028833
TFDP1_HUMAN	TFDP1	physical	29028833
PCGF6_HUMAN	PCGF6	physical	29028833
RING1_HUMAN	RING1	physical	29028833
RING2_HUMAN	RNF2	physical	29028833
CBX3_HUMAN	CBX3	physical	29028833
LMBL2_HUMAN	L3MBTL2	physical	29028833
RYBP_HUMAN	RYBP	physical	29028833
YAF2_HUMAN	YAF2	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.

Regulatory Network of MAX_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Max is acetylated by p300 at several nuclear localization residues."; Faiola F., Wu Y.-T., Pan S., Zhang K., Farina A., Martinez E.; Biochem. J. 403:397-407(2007). Cited for: ACETYLATION AT LYS-66; LYS-153 AND LYS-154, AND MUTAGENESIS OF LYS-66;LYS-153 AND LYS-154.	17217336 [Abstract]
Phosphorylation
Reference	PubMed
"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-2 AND SER-11, AND MASSSPECTROMETRY.	19413330 [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 SER-2, 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 SER-2 AND SER-11, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-123, AND MASSSPECTROMETRY.	15592455 [Abstract]