MTPN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MTPN_HUMAN
• UniProt AC: P58546
• Protein Name: Myotrophin
• Gene Name: MTPN
• Organism: Homo sapiens (Human).
• Sequence Length: 118
• Subcellular Localization: Cytoplasm . Nucleus. Cytoplasm, perinuclear region.
• Protein Description: Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity (By similarity). Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy..
• Protein Sequence: MCDKEFMWALKNGDLDEVKDYVAKGEDVNRTLEGGRKPLHYAADCGQLEILEFLLLKGADINAPDKHHITPLLSAVYEGHVSCVKLLLSKGADKTVKGPDGLTAFEATDNQAIKALLQ

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
2	Acetylation	------MCDKEFMWA ------CCCHHHHHH	11.71	-
4	Acetylation	----MCDKEFMWALK ----CCCHHHHHHHH	48.18	19608861
4	Ubiquitination	----MCDKEFMWALK ----CCCHHHHHHHH	48.18	19608861
4	2-Hydroxyisobutyrylation	----MCDKEFMWALK ----CCCHHHHHHHH	48.18	-
11	Acetylation	KEFMWALKNGDLDEV HHHHHHHHCCCHHHH	51.65	19608861
11	Ubiquitination	KEFMWALKNGDLDEV HHHHHHHHCCCHHHH	51.65	21890473
19	2-Hydroxyisobutyrylation	NGDLDEVKDYVAKGE CCCHHHHHHHHHCCC	41.09	-
19	Ubiquitination	NGDLDEVKDYVAKGE CCCHHHHHHHHHCCC	41.09	-
19	Sumoylation	NGDLDEVKDYVAKGE CCCHHHHHHHHHCCC	41.09	-
19	Acetylation	NGDLDEVKDYVAKGE CCCHHHHHHHHHCCC	41.09	26051181
21	Phosphorylation	DLDEVKDYVAKGEDV CHHHHHHHHHCCCCC	9.15	28152594
24	Ubiquitination	EVKDYVAKGEDVNRT HHHHHHHCCCCCCCH	53.43	21906983
24	Acetylation	EVKDYVAKGEDVNRT HHHHHHHCCCCCCCH	53.43	19608861
31	Phosphorylation	KGEDVNRTLEGGRKP CCCCCCCHHCCCCCC	24.77	23401153
66	Acetylation	ADINAPDKHHITPLL CCCCCCCHHCCHHHH	35.70	23749302
66	Ubiquitination	ADINAPDKHHITPLL CCCCCCCHHCCHHHH	35.70	-
66	Malonylation	ADINAPDKHHITPLL CCCCCCCHHCCHHHH	35.70	26320211
89	Phosphorylation	SCVKLLLSKGADKTV HHHHHHHHCCCCCCE	29.07	28348404
90	2-Hydroxyisobutyrylation	CVKLLLSKGADKTVK HHHHHHHCCCCCCEE	59.07	-
90	Succinylation	CVKLLLSKGADKTVK HHHHHHHCCCCCCEE	59.07	23954790
90	Ubiquitination	CVKLLLSKGADKTVK HHHHHHHCCCCCCEE	59.07	-
94	2-Hydroxyisobutyrylation	LLSKGADKTVKGPDG HHHCCCCCCEECCCC	55.47	-
97	Ubiquitination	KGADKTVKGPDGLTA CCCCCCEECCCCCEE	70.70	19608861
97	Acetylation	KGADKTVKGPDGLTA CCCCCCEECCCCCEE	70.70	23954790
114	Ubiquitination	ATDNQAIKALLQ--- CCCHHHHHHHHC---	35.68	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of MTPN_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MTPN_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 MTPN_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TF65_HUMAN	RELA	physical	11971907
NFKB1_HUMAN	NFKB1	physical	11971907
REL_HUMAN	REL	physical	11971907
NPL4_HUMAN	NPLOC4	physical	22939629
DPY30_HUMAN	DPY30	physical	26344197
GARS_HUMAN	GARS	physical	26344197
NPL4_HUMAN	NPLOC4	physical	26344197
PI42A_HUMAN	PIP4K2A	physical	26344197
PI42C_HUMAN	PIP4K2C	physical	26344197
UBA1_HUMAN	UBA1	physical	26344197

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.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2; LYS-4; LYS-11; LYS-24 ANDLYS-97, AND MASS SPECTROMETRY.
PubMed: 19608861