dbPTM

MARE2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MARE2_HUMAN
UniProt AC	Q15555
Protein Name	Microtubule-associated protein RP/EB family member 2
Gene Name	MAPRE2
Organism	Homo sapiens (Human).
Sequence Length	327
Subcellular Localization	Cytoplasm, cytoskeleton . Associated with the microtubule network. Accumulates at the plus end of microtubules.
Protein Description	May be involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration (By similarity)..
Protein Sequence	MPGPTQTLSPNGENNNDIIQDNNGTIIPFRKHTVRGERSYSWGMAVNVYSTSITQETMSRHDIIAWVNDIVSLNYTKVEQLCSGAAYCQFMDMLFPGCISLKKVKFQAKLEHEYIHNFKLLQASFKRMNVDKVIPVEKLVKGRFQDNLDFIQWFKKFYDANYDGKEYDPVEARQGQDAIPPPDPGEQIFNLPKKSHHANSPTAGAAKSSPAAKPGSTPSRPSSAKRASSSGSASKSDKDLETQVIQLNEQVHSLKLALEGVEKERDFYFGKLREIELLCQEHGQENDDLVQRLMDILYASEEHEGHTEEPEAEEQAHEQQPPQQEEY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2 (in isoform 5)	Acetylation	-	58.43	22814378
5	Phosphorylation	---MPGPTQTLSPNG ---CCCCCCCCCCCC	39.85	29255136
7	Phosphorylation	-MPGPTQTLSPNGEN -CCCCCCCCCCCCCC	31.51	23401153
9	Phosphorylation	PGPTQTLSPNGENNN CCCCCCCCCCCCCCC	21.51	23401153
25	Phosphorylation	IIQDNNGTIIPFRKH CEECCCCCEEECCCC	20.18	26074081
33	Phosphorylation	IIPFRKHTVRGERSY EEECCCCEECCEECC	18.22	-
39	Phosphorylation	HTVRGERSYSWGMAV CEECCEECCEEEEEE	21.15	29978859
40	Phosphorylation	TVRGERSYSWGMAVN EECCEECCEEEEEEE	18.05	29978859
41	Phosphorylation	VRGERSYSWGMAVNV ECCEECCEEEEEEEE	20.57	29978859
49	Phosphorylation	WGMAVNVYSTSITQE EEEEEEEEECCCCHH	10.88	29978859
50	Phosphorylation	GMAVNVYSTSITQET EEEEEEEECCCCHHH	16.05	28851738
51	Phosphorylation	MAVNVYSTSITQETM EEEEEEECCCCHHHH	13.37	27732954
52	Phosphorylation	AVNVYSTSITQETMS EEEEEECCCCHHHHC	20.07	27732954
54	Phosphorylation	NVYSTSITQETMSRH EEEECCCCHHHHCHH	21.81	28851738
57	Phosphorylation	STSITQETMSRHDII ECCCCHHHHCHHHHH	15.61	28851738
59	Phosphorylation	SITQETMSRHDIIAW CCCHHHHCHHHHHHH	33.61	28851738
76	Ubiquitination	DIVSLNYTKVEQLCS HHHCCCCCCHHHHHC	27.78	-
83	Ubiquitination	TKVEQLCSGAAYCQF CCHHHHHCCHHHHHH	39.81	-
89	Ubiquitination	CSGAAYCQFMDMLFP HCCHHHHHHHHHHCC	24.83	-
95	Ubiquitination	CQFMDMLFPGCISLK HHHHHHHCCCCEEEC	3.82	-
98	Ubiquitination	MDMLFPGCISLKKVK HHHHCCCCEEECEEE	1.62	-
102	Ubiquitination	FPGCISLKKVKFQAK CCCCEEECEEEEEEE	49.05	21890473
109	Acetylation	KKVKFQAKLEHEYIH CEEEEEEECCCHHHH	43.56	26051181
109	Ubiquitination	KKVKFQAKLEHEYIH CEEEEEEECCCHHHH	43.56	-
112	Ubiquitination	KFQAKLEHEYIHNFK EEEEECCCHHHHHHH	43.53	-
113	Ubiquitination	FQAKLEHEYIHNFKL EEEECCCHHHHHHHH	36.49	-
119	Ubiquitination	HEYIHNFKLLQASFK CHHHHHHHHHHHHHH	54.31	-
119	Acetylation	HEYIHNFKLLQASFK CHHHHHHHHHHHHHH	54.31	25953088
122	Ubiquitination	IHNFKLLQASFKRMN HHHHHHHHHHHHHCC	45.45	-
124	Phosphorylation	NFKLLQASFKRMNVD HHHHHHHHHHHCCCC	20.52	30108239
126	Acetylation	KLLQASFKRMNVDKV HHHHHHHHHCCCCCE	48.52	25953088
126	Malonylation	KLLQASFKRMNVDKV HHHHHHHHHCCCCCE	48.52	26320211
126	Ubiquitination	KLLQASFKRMNVDKV HHHHHHHHHCCCCCE	48.52	-
132	Ubiquitination	FKRMNVDKVIPVEKL HHHCCCCCEEEHHHH	37.47	-
138	Acetylation	DKVIPVEKLVKGRFQ CCEEEHHHHHCCCCC	59.83	25953088
138	Ubiquitination	DKVIPVEKLVKGRFQ CCEEEHHHHHCCCCC	59.83	-
141	Ubiquitination	IPVEKLVKGRFQDNL EEHHHHHCCCCCCCC	55.60	-
143	Ubiquitination	VEKLVKGRFQDNLDF HHHHHCCCCCCCCHH	21.97	21890473
143	Ubiquitination	VEKLVKGRFQDNLDF HHHHHCCCCCCCCHH	21.97	21890473
151	Ubiquitination	FQDNLDFIQWFKKFY CCCCCHHHHHHHHHH	3.37	-
155 (in isoform 1)	Ubiquitination	-	38.73	21890473
155 (in isoform 2)	Ubiquitination	-	38.73	21890473
155	Ubiquitination	LDFIQWFKKFYDANY CHHHHHHHHHHCCCC	38.73	21890473
156	Ubiquitination	DFIQWFKKFYDANYD HHHHHHHHHHCCCCC	39.42	-
158	Phosphorylation	IQWFKKFYDANYDGK HHHHHHHHCCCCCCC	24.03	29496907
162	Phosphorylation	KKFYDANYDGKEYDP HHHHCCCCCCCCCCC	28.00	29978859
165	Ubiquitination	YDANYDGKEYDPVEA HCCCCCCCCCCCCHH	50.64	-
165	Sumoylation	YDANYDGKEYDPVEA HCCCCCCCCCCCCHH	50.64	-
167	Phosphorylation	ANYDGKEYDPVEARQ CCCCCCCCCCCHHCC	29.09	25159151
193	Ubiquitination	EQIFNLPKKSHHANS HHHCCCCCCCCCCCC	70.81	-
194	Ubiquitination	QIFNLPKKSHHANSP HHCCCCCCCCCCCCC	53.75	-
195	Phosphorylation	IFNLPKKSHHANSPT HCCCCCCCCCCCCCC	26.99	29691806
200	Phosphorylation	KKSHHANSPTAGAAK CCCCCCCCCCCCCCC	25.14	25159151
202	Phosphorylation	SHHANSPTAGAAKSS CCCCCCCCCCCCCCC	37.23	28176443
207	Ubiquitination	SPTAGAAKSSPAAKP CCCCCCCCCCCCCCC	51.43	-
208	Phosphorylation	PTAGAAKSSPAAKPG CCCCCCCCCCCCCCC	36.51	23401153
209	Phosphorylation	TAGAAKSSPAAKPGS CCCCCCCCCCCCCCC	20.18	25159151
213	Ubiquitination	AKSSPAAKPGSTPSR CCCCCCCCCCCCCCC	52.60	-
213	Acetylation	AKSSPAAKPGSTPSR CCCCCCCCCCCCCCC	52.60	25953088
216	Phosphorylation	SPAAKPGSTPSRPSS CCCCCCCCCCCCCCC	45.75	23401153
216	O-linked_Glycosylation	SPAAKPGSTPSRPSS CCCCCCCCCCCCCCC	45.75	28411811
217	Phosphorylation	PAAKPGSTPSRPSSA CCCCCCCCCCCCCCC	31.06	25159151
218	Ubiquitination	AAKPGSTPSRPSSAK CCCCCCCCCCCCCCC	30.00	21890473
219	Phosphorylation	AKPGSTPSRPSSAKR CCCCCCCCCCCCCCC	57.84	25159151
222	Phosphorylation	GSTPSRPSSAKRASS CCCCCCCCCCCCCCC	41.64	25159151
223	Phosphorylation	STPSRPSSAKRASSS CCCCCCCCCCCCCCC	40.26	25159151
225	Acetylation	PSRPSSAKRASSSGS CCCCCCCCCCCCCCC	50.90	12435305
228	Acetylation	PSSAKRASSSGSASK CCCCCCCCCCCCCCC	29.12	-
228	Ubiquitination	PSSAKRASSSGSASK CCCCCCCCCCCCCCC	29.12	-
228	Phosphorylation	PSSAKRASSSGSASK CCCCCCCCCCCCCCC	29.12	26657352
229	Phosphorylation	SSAKRASSSGSASKS CCCCCCCCCCCCCCC	37.42	23401153
230	Phosphorylation	SAKRASSSGSASKSD CCCCCCCCCCCCCCC	33.98	29978859
232	Phosphorylation	KRASSSGSASKSDKD CCCCCCCCCCCCCHH	31.17	28464451
234	Phosphorylation	ASSSGSASKSDKDLE CCCCCCCCCCCHHHH	34.10	18669648
235	Ubiquitination	SSSGSASKSDKDLET CCCCCCCCCCHHHHH	63.49	-
236	Phosphorylation	SSGSASKSDKDLETQ CCCCCCCCCHHHHHH	47.61	28464451
238	Acetylation	GSASKSDKDLETQVI CCCCCCCHHHHHHHH	71.89	25953088
238	Ubiquitination	GSASKSDKDLETQVI CCCCCCCHHHHHHHH	71.89	-
242	Phosphorylation	KSDKDLETQVIQLNE CCCHHHHHHHHHHHH	35.12	28464451
253	Phosphorylation	QLNEQVHSLKLALEG HHHHHHHHHHHHHHH	28.48	30576142
255	Ubiquitination	NEQVHSLKLALEGVE HHHHHHHHHHHHHHH	34.43	-
259	Ubiquitination	HSLKLALEGVEKERD HHHHHHHHHHHHHHH	56.43	21890473
259	Ubiquitination	HSLKLALEGVEKERD HHHHHHHHHHHHHHH	56.43	21890473
263	Ubiquitination	LALEGVEKERDFYFG HHHHHHHHHHHCHHH	56.49	-
263	Acetylation	LALEGVEKERDFYFG HHHHHHHHHHHCHHH	56.49	25953088
271	Acetylation	ERDFYFGKLREIELL HHHCHHHHHHHHHHH	34.18	23236377
271	Ubiquitination	ERDFYFGKLREIELL HHHCHHHHHHHHHHH	34.18	21890473
271 (in isoform 1)	Ubiquitination	-	34.18	21890473
327	Phosphorylation	QPPQQEEY------- CCCCCCCC-------	24.09	27642862

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
236	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MARE2_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 MARE2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NIF3L_HUMAN	NIF3L1	physical	16189514
MARE2_HUMAN	MAPRE2	physical	16189514
MARE3_HUMAN	MAPRE3	physical	16189514
APC_HUMAN	APC	physical	11470413
A4_HUMAN	APP	physical	21832049
MARE2_HUMAN	MAPRE2	physical	25416956
MARE1_HUMAN	MAPRE1	physical	25416956
PAXI1_HUMAN	PAXIP1	physical	25416956
THIOM_HUMAN	TXN2	physical	25416956
CRAC1_HUMAN	CRTAC1	physical	25416956
MCM6_HUMAN	MCM6	physical	26344197
HSF1_HUMAN	HSF1	physical	27173435
TC1D2_HUMAN	TCTEX1D2	physical	27173435

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 MARE2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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 LYS-271, AND MASS SPECTROMETRY.	19608861 [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-9, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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 SER-208 AND SER-219, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219 AND SER-223, ANDMASS SPECTROMETRY.	17287340 [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-200, 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-167, AND MASSSPECTROMETRY.	15592455 [Abstract]