dbPTM

MOT4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MOT4_HUMAN
UniProt AC	O15427
Protein Name	Monocarboxylate transporter 4
Gene Name	SLC16A3
Organism	Homo sapiens (Human).
Sequence Length	465
Subcellular Localization	Cell membrane Multi-pass membrane protein.
Protein Description	Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate (By similarity)..
Protein Sequence	MGGAVVDEGPTGVKAPDGGWGWAVLFGCFVITGFSYAFPKAVSVFFKELIQEFGIGYSDTAWISSILLAMLYGTGPLCSVCVNRFGCRPVMLVGGLFASLGMVAASFCRSIIQVYLTTGVITGLGLALNFQPSLIMLNRYFSKRRPMANGLAAAGSPVFLCALSPLGQLLQDRYGWRGGFLILGGLLLNCCVCAALMRPLVVTAQPGSGPPRPSRRLLDLSVFRDRGFVLYAVAASVMVLGLFVPPVFVVSYAKDLGVPDTKAAFLLTILGFIDIFARPAAGFVAGLGKVRPYSVYLFSFSMFFNGLADLAGSTAGDYGGLVVFCIFFGISYGMVGALQFEVLMAIVGTHKFSSAIGLVLLMEAVAVLVGPPSGGKLLDATHVYMYVFILAGAEVLTSSLILLLGNFFCIRKKPKEPQPEVAAAEEEKLHKPPADSGVDLREVEHFLKAEPEKNGEVVHTPETSV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
35	Phosphorylation	CFVITGFSYAFPKAV EEEHHCCCCCCHHHH	19.52	-
36	Phosphorylation	FVITGFSYAFPKAVS EEHHCCCCCCHHHHH	15.25	-
110	Phosphorylation	VAASFCRSIIQVYLT HHHHHHHHHHHHHHH	25.81	22210691
115	Phosphorylation	CRSIIQVYLTTGVIT HHHHHHHHHHHCHHH	5.07	27174698
117	Phosphorylation	SIIQVYLTTGVITGL HHHHHHHHHCHHHHH	12.10	27174698
118	Phosphorylation	IIQVYLTTGVITGLG HHHHHHHHCHHHHHH	27.19	27174698
122	Phosphorylation	YLTTGVITGLGLALN HHHHCHHHHHHHHHH	24.77	27174698
133	Phosphorylation	LALNFQPSLIMLNRY HHHHCCCHHHHHHHH	21.53	27174698
161	S-palmitoylation	AGSPVFLCALSPLGQ CCCCEEEEEECHHHH	2.13	29575903
254	Sumoylation	VFVVSYAKDLGVPDT EEEEHHHHHHCCCCH	45.30	-
262	Sumoylation	DLGVPDTKAAFLLTI HHCCCCHHHHHHHHH	45.13	-
415	Ubiquitination	FCIRKKPKEPQPEVA HHCCCCCCCCCCCCC	85.67	21906983
428	Ubiquitination	VAAAEEEKLHKPPAD CCHHHHHHHCCCCCC	60.20	21906983
431	Ubiquitination	AEEEKLHKPPADSGV HHHHHHCCCCCCCCC	64.23	21906983
431	2-Hydroxyisobutyrylation	AEEEKLHKPPADSGV HHHHHHCCCCCCCCC	64.23	-
436	Phosphorylation	LHKPPADSGVDLREV HCCCCCCCCCCHHHH	42.70	29255136
448	Sumoylation	REVEHFLKAEPEKNG HHHHHHHHCCCCCCC	50.16	-
448	Ubiquitination	REVEHFLKAEPEKNG HHHHHHHHCCCCCCC	50.16	21906983
448	Acetylation	REVEHFLKAEPEKNG HHHHHHHHCCCCCCC	50.16	27452117
453	Ubiquitination	FLKAEPEKNGEVVHT HHHCCCCCCCCCCCC	79.54	21906983
460	Phosphorylation	KNGEVVHTPETSV-- CCCCCCCCCCCCC--	15.94	28355574
463	Phosphorylation	EVVHTPETSV----- CCCCCCCCCC-----	35.67	22167270
464	Phosphorylation	VVHTPETSV------ CCCCCCCCC------	24.94	22167270

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 MOT4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MOT4_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 MOT4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BANP_HUMAN	BANP	physical	25416956
NR2CA_HUMAN	NR2C2AP	physical	25416956
FAM9B_HUMAN	FAM9B	physical	25416956

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
DB01440	Gamma Hydroxybutyric Acid
DB00627	Niacin
DB00119	Pyruvic acid

Regulatory Network of MOT4_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 THR-460 AND SER-464, ANDMASS SPECTROMETRY.	18669648 [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 THR-460 AND SER-464, ANDMASS SPECTROMETRY.	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-436; THR-460 ANDSER-464, AND MASS SPECTROMETRY.	17081983 [Abstract]