dbPTM

MK15_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MK15_HUMAN
UniProt AC	Q8TD08
Protein Name	Mitogen-activated protein kinase 15 {ECO:0000305}
Gene Name	MAPK15 {ECO:0000312\|HGNC:HGNC:24667}
Organism	Homo sapiens (Human).
Sequence Length	544
Subcellular Localization	Cytoplasm, cytoskeleton, cilium basal body . Cell junction, tight junction . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Cytoplasmic vesicle, autophagosome . Golgi apparatus . Nucleus . Cytoplasm . Cytoplasm, cytoskelet
Protein Description	Atypical MAPK protein that regulates several process such as autophagy, ciliogenesis, protein trafficking/secretion and genome integrity, in a kinase activity-dependent manner. [PubMed: 22948227]
Protein Sequence	MCTVVDPRIVRRYLLRRQLGQGAYGIVWKAVDRRTGEVVAIKKIFDAFRDKTDAQRTFREITLLQEFGDHPNIISLLDVIRAENDRDIYLVFEFMDTDLNAVIRKGGLLQDVHVRSIFYQLLRATRFLHSGHVVHRDQKPSNVLLDANCTVKLCDFGLARSLGDLPEGPEDQAVTEYVATRWYRAPEVLLSSHRYTLGVDMWSLGCILGEMLRGRPLFPGTSTLHQLELILETIPPPSEEDLLALGSGCRASVLHQLGSRPRQTLDALLPPDTSPEALDLLRRLLVFAPDKRLSATQALQHPYVQRFHCPSDEWAREADVRPRAHEGVQLSVPEYRSRVYQMILECGGSSGTSREKGPEGVSPSQAHLHKPRADPQLPSRTPVQGPRPRPQSSPGHDPAEHESPRAAKNVPRQNSAPLLQTALLGNGERPPGAKEAPPLTLSLVKPSGRGAAPSLTSQAAAQVANQALIRGDWNRGGGVRVASVQQVPPRLPPEARPGRRMFSTSALQGAQGGARALLGGYSQAYGTVCHSALGHLPLLEGHHV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
109 (in isoform 3)	Phosphorylation	-	4.64	23090842
111 (in isoform 3)	Phosphorylation	-	32.24	23090842
114 (in isoform 3)	Phosphorylation	-	5.29	23090842
175	Phosphorylation	GPEDQAVTEYVATRW CCHHHHHHHHHHHCH	25.31	16484222
177	Phosphorylation	EDQAVTEYVATRWYR HHHHHHHHHHHCHHC	5.99	16484222
180	Phosphorylation	AVTEYVATRWYRAPE HHHHHHHHCHHCCHH	16.22	26074081
192	Phosphorylation	APEVLLSSHRYTLGV CHHHHHCCCCCCCCC	16.38	16336213
331	Phosphorylation	AHEGVQLSVPEYRSR CCCCCCCCCHHHHHH	20.66	16336213
340	Phosphorylation	PEYRSRVYQMILECG HHHHHHHHHHHHHCC	7.40	-
352	Phosphorylation	ECGGSSGTSREKGPE HCCCCCCCCCCCCCC	26.93	16336213
362	Phosphorylation	EKGPEGVSPSQAHLH CCCCCCCCHHHHHCC	29.68	16336213
379	Phosphorylation	RADPQLPSRTPVQGP CCCCCCCCCCCCCCC	58.33	16336213
381	Phosphorylation	DPQLPSRTPVQGPRP CCCCCCCCCCCCCCC	31.95	16336213
392	Phosphorylation	GPRPRPQSSPGHDPA CCCCCCCCCCCCCCC	40.98	27251275
393	Phosphorylation	PRPRPQSSPGHDPAE CCCCCCCCCCCCCCC	29.65	27251275
415	Phosphorylation	KNVPRQNSAPLLQTA HCCCCCCCCCHHHHH	23.95	27251275
440	Phosphorylation	AKEAPPLTLSLVKPS CCCCCCEEEEEECCC	21.78	26699800
442	Phosphorylation	EAPPLTLSLVKPSGR CCCCEEEEEECCCCC	26.36	26699800
449	Methylation	SLVKPSGRGAAPSLT EEECCCCCCCCCCHH	35.60	24129315

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
175	T	Phosphorylation	Kinase	MAPK15	Q8TD08	GPS
177	Y	Phosphorylation	Kinase	MAPK15	Q8TD08	GPS
192	S	Phosphorylation	Kinase	MAPK15	Q8TD08	GPS
331	S	Phosphorylation	Kinase	MAPK15	Q8TD08	GPS
352	T	Phosphorylation	Kinase	MAPK15	Q8TD08	GPS
362	S	Phosphorylation	Kinase	MAPK15	Q8TD08	GPS
379	S	Phosphorylation	Kinase	MAPK15	Q8TD08	GPS
381	T	Phosphorylation	Kinase	MAPK15	Q8TD08	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
175	T	Phosphorylation		11875070
Autophosphorylated on Thr-175 and Tyr-177; activates the enzyme.

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 MK15_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CLIC3_HUMAN	CLIC3	physical	9880541
PCNA_HUMAN	PCNA	physical	20733054
MLP3B_HUMAN	MAP1LC3B	physical	22948227
GBRAP_MOUSE	Gabarap	physical	22948227
GBRL1_MOUSE	Gabarapl1	physical	22948227
MK12_HUMAN	MAPK12	physical	23602568
ESYT2_HUMAN	ESYT2	physical	23602568
TRFL_HUMAN	LTF	physical	23602568
WDR81_HUMAN	WDR81	physical	23602568
CAC1H_HUMAN	CACNA1H	physical	23602568
RBM14_HUMAN	RBM14	physical	23602568
PIGR_HUMAN	PIGR	physical	23602568
B2MG_HUMAN	B2M	physical	23602568
NAMPT_HUMAN	NAMPT	physical	28514442
TCPB_HUMAN	CCT2	physical	28514442
TCPG_HUMAN	CCT3	physical	28514442
TCPW_HUMAN	CCT6B	physical	28514442

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 MK15_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-177; SER-392 ANDSER-415, AND MASS SPECTROMETRY.	19369195 [Abstract]
"ERK8, a new member of the mitogen-activated protein kinase family."; Abe M.K., Saelzler M.P., Espinosa R. III, Kahle K.T., Hershenson M.B.,Le Beau M.M., Rosner M.R.; J. Biol. Chem. 277:16733-16743(2002). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,INTERACTION WITH CSK, MUTAGENESIS OF LYS-42; THR-175 AND TYR-177,PHOSPHORYLATION AT THR-175 AND TYR-177, CHARACTERIZATION, ANDFUNCTION.	11875070 [Abstract]