dbPTM

MNT_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MNT_HUMAN
UniProt AC	Q99583
Protein Name	Max-binding protein MNT
Gene Name	MNT
Organism	Homo sapiens (Human).
Sequence Length	582
Subcellular Localization	Nucleus.
Protein Description	Binds DNA as a heterodimer with MAX and represses transcription. Binds to the canonical E box sequence 5'-CACGTG-3' and, with higher affinity, to 5'-CACGCG-3'..
Protein Sequence	MSIETLLEAARFLEWQAQQQQRAREEQERLRLEQEREQEQKKANSLARLAHTLPVEEPRMEAPPLPLSPPAPPPAPPPPLATPAPLTVIPIPVVTNSPQPLPPPPPLPAAAQPLPLAPRQPALVGAPGLSIKEPAPLPSRPQVPTPAPLLPDSKATIPPNGSPKPLQPLPTPVLTIAPHPGVQPQLAPQQPPPPTLGTLKLAPAEEVKSSEQKKRPGGIGTREVHNKLEKNRRAHLKECFETLKRNIPNVDDKKTSNLSVLRTALRYIQSLKRKEKEYEHEMERLAREKIATQQRLAELKHELSQWMDVLEIDRVLRQTGQPEDDQASTSTASEGEDNIDEDMEEDRAGLGPPKLSHRPQPELLKSTLPPPSTTPAPLPPHPHPHPHSVALPPAHLPVQQQQPQQKTPLPAPPPPPAAPAQTLVPAPAHLVATAGGGSTVIAHTATTHASVIQTVNHVLQGPGGKHIAHIAPSAPSPAVQLAPATPPIGHITVHPATLNHVAHLGSQLPLYPQPVAVSHIAHTLSHQQVNGTAGLGPPATVMAKPAVGAQVVHHPQLVGQTVLNPVTMVTMPSFPVSTLKLA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSIETLLEA ------CCHHHHHHH	29.18	22814378
2	Phosphorylation	------MSIETLLEA ------CCHHHHHHH	29.18	23401153
5	Phosphorylation	---MSIETLLEAARF ---CCHHHHHHHHHH	34.67	23401153
156	Phosphorylation	LLPDSKATIPPNGSP CCCCCCCCCCCCCCC	37.44	17192257
162	Phosphorylation	ATIPPNGSPKPLQPL CCCCCCCCCCCCCCC	36.07	20068231
171	Phosphorylation	KPLQPLPTPVLTIAP CCCCCCCCCEEEECC	33.44	27251275
175	Phosphorylation	PLPTPVLTIAPHPGV CCCCCEEEECCCCCC	18.48	22210691
209	Phosphorylation	APAEEVKSSEQKKRP CCHHHHCCCCCCCCC	44.26	25627689
210	Phosphorylation	PAEEVKSSEQKKRPG CHHHHCCCCCCCCCC	38.03	25159151
259	Phosphorylation	DKKTSNLSVLRTALR CCHHCCHHHHHHHHH	24.29	19664995
267	Phosphorylation	VLRTALRYIQSLKRK HHHHHHHHHHHHHHH	12.26	27794612
270	Phosphorylation	TALRYIQSLKRKEKE HHHHHHHHHHHHHHH	26.71	27794612
328	Phosphorylation	QPEDDQASTSTASEG CCCCCCCCCCCCCCC	19.77	23909892
329	Phosphorylation	PEDDQASTSTASEGE CCCCCCCCCCCCCCC	32.86	23909892
330	Phosphorylation	EDDQASTSTASEGED CCCCCCCCCCCCCCC	21.34	23909892
331	Phosphorylation	DDQASTSTASEGEDN CCCCCCCCCCCCCCC	34.00	23909892
333	Phosphorylation	QASTSTASEGEDNID CCCCCCCCCCCCCCC	46.34	23909892
407	O-linked_Glycosylation	QQQPQQKTPLPAPPP CCCCCCCCCCCCCCC	26.22	29351928
444	O-linked_Glycosylation	GSTVIAHTATTHASV CCEEEEEECCCCHHH	19.37	OGP
450	O-linked_Glycosylation	HTATTHASVIQTVNH EECCCCHHHHHHHHH	16.49	29351928

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 MNT_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MAX_HUMAN	MAX	physical	9184233
MNT_HUMAN	MNT	physical	9184233
SIN3A_HUMAN	SIN3A	physical	9184233
MLX_HUMAN	MLX	physical	11230181
MLX_HUMAN	MLX	physical	10918583
SIN3A_MOUSE	Sin3a	physical	10918583
MNT_HUMAN	MNT	physical	10918583
HDAC1_HUMAN	HDAC1	physical	18271930
MYC_HUMAN	MYC	physical	18271930
MD1L1_HUMAN	MAD1L1	physical	18271930
MAX_HUMAN	MAX	physical	18271930
UBE3A_HUMAN	UBE3A	physical	26506232

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 MNT_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 THR-156, AND MASSSPECTROMETRY.	18691976 [Abstract]