dbPTM

AMOT_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AMOT_HUMAN
UniProt AC	Q4VCS5
Protein Name	Angiomotin
Gene Name	AMOT
Organism	Homo sapiens (Human).
Sequence Length	1084
Subcellular Localization	Cell junction, tight junction . Localized on the cell surface. May act as a transmembrane protein.
Protein Description	Plays a central role in tight junction maintenance via the complex formed with ARHGAP17, which acts by regulating the uptake of polarity proteins at tight junctions. Appears to regulate endothelial cell migration and tube formation. May also play a role in the assembly of endothelial cell-cell junctions..
Protein Sequence	MRNSEEQPSGGTTVLQRLLQEQLRYGNPSENRSLLAIHQQATGNGPPFPSGSGNPGPQSDVLSPQDHHQQLVAHAARQEPQGQEIQSENLIMEKQLSPRMQNNEELPTYEEAKVQSQYFRGQQHASVGAAFYVTGVTNQKMRTEGRPSVQRLNPGKMHQDEGLRDLKQGHVRSLSERLMQMSLATSGVKAHPPVTSAPLSPPQPNDLYKNPTSSSEFYKAQGPLPNQHSLKGMEHRGPPPEYPFKGMPPQSVVCKPQEPGHFYSEHRLNQPGRTEGQLMRYQHPPEYGAARPAQDISLPLSARNSQPHSPTSSLTSGGSLPLLQSPPSTRLSPARHPLVPNQGDHSAHLPRPQQHFLPNQAHQGDHYRLSQPGLSQQQQQQQQQHHHHHHHQQQQQQQPQQQPGEAYSAMPRAQPSSASYQPVPADPFAIVSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNCQPTNVSEYNAAALMELLREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSCMRPAKSLMSISNAGSGLLSHSSTLTGSPIMEEKRDDKSWKGSLGILLGGDYRAEYVPSTPSPVPPSTPLLSAHSKTGSRDCSTQTERGTESNKTAAVAPISVPAPVAAAATAAAITATAATITTTMVAAAPVAVAAAAAPAAAAAPSPATAAATAAAVSPAAAGQIPAAASVASAAAVAPSAAAAAAVQVAPAAPAPVPAPALVPVPAPAAAQASAPAQTQAPTSAPAVAPTPAPTPTPAVAQAEVPASPATGPGPHRLSIPSLTCNPDKTDGPVFHSNTLERKTPIQILGQEPDAEMVEYLI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MRNSEEQPSGG ----CCCCCCCCCCH	49.06	23401153
8 (in isoform 2)	Phosphorylation	-	37.92	22210691
9	Phosphorylation	RNSEEQPSGGTTVLQ CCCCCCCCCHHHHHH	49.93	23401153
12	Phosphorylation	EEQPSGGTTVLQRLL CCCCCCHHHHHHHHH	19.77	23401153
13	Phosphorylation	EQPSGGTTVLQRLLQ CCCCCHHHHHHHHHH	23.61	28270605
24	Methylation	RLLQEQLRYGNPSEN HHHHHHHHHCCCCCC	36.69	-
33 (in isoform 2)	Phosphorylation	-	39.04	22210691
55	Ubiquitination	FPSGSGNPGPQSDVL CCCCCCCCCCHHHCC	60.41	32015554
72	Ubiquitination	QDHHQQLVAHAARQE CHHHHHHHHHHHHCC	2.97	32015554
87	Ubiquitination	PQGQEIQSENLIMEK CCCCCCHHHHHHHHH	33.83	32015554
94	Ubiquitination	SENLIMEKQLSPRMQ HHHHHHHHCCCHHHC	38.88	23000965
94 (in isoform 1)	Ubiquitination	-	38.88	21890473
97	Phosphorylation	LIMEKQLSPRMQNNE HHHHHCCCHHHCCCC	14.15	17322306
100	Oxidation	EKQLSPRMQNNEELP HHCCCHHHCCCCCCC	5.93	17322306
108	Phosphorylation	QNNEELPTYEEAKVQ CCCCCCCCHHHHHHH	57.07	28796482
109	Phosphorylation	NNEELPTYEEAKVQS CCCCCCCHHHHHHHH	15.16	28796482
111	Ubiquitination	EELPTYEEAKVQSQY CCCCCHHHHHHHHHH	43.29	32015554
113	Ubiquitination	LPTYEEAKVQSQYFR CCCHHHHHHHHHHHC	44.05	22053931
113 (in isoform 1)	Ubiquitination	-	44.05	21890473
118	Phosphorylation	EAKVQSQYFRGQQHA HHHHHHHHHCCCCCC	10.65	29496907
132	Phosphorylation	ASVGAAFYVTGVTNQ CCCCEEEEEECCCCH	7.74	27642862
134	Ubiquitination	VGAAFYVTGVTNQKM CCEEEEEECCCCHHC	17.98	32015554
140	Ubiquitination	VTGVTNQKMRTEGRP EECCCCHHCCCCCCC	32.21	32015554
144	Ubiquitination	TNQKMRTEGRPSVQR CCHHCCCCCCCCCCC	42.72	29967540
156	Ubiquitination	VQRLNPGKMHQDEGL CCCCCCCCCCCCHHH	34.17	29967540
167	Ubiquitination	DEGLRDLKQGHVRSL CHHHHHHHHHHHHHH	59.53	32015554
175	Phosphorylation	QGHVRSLSERLMQMS HHHHHHHHHHHHHHH	23.16	57399011
176	Ubiquitination	GHVRSLSERLMQMSL HHHHHHHHHHHHHHH	55.94	32015554
182	O-linked_Glycosylation	SERLMQMSLATSGVK HHHHHHHHHHCCCCC	9.65	28657654
182	Phosphorylation	SERLMQMSLATSGVK HHHHHHHHHHCCCCC	9.65	30377224
195	O-linked_Glycosylation	VKAHPPVTSAPLSPP CCCCCCCCCCCCCCC	25.58	28657654
195	Phosphorylation	VKAHPPVTSAPLSPP CCCCCCCCCCCCCCC	25.58	29978859
196	Phosphorylation	KAHPPVTSAPLSPPQ CCCCCCCCCCCCCCC	28.29	29978859
196	Ubiquitination	KAHPPVTSAPLSPPQ CCCCCCCCCCCCCCC	28.29	32015554
200	Phosphorylation	PVTSAPLSPPQPNDL CCCCCCCCCCCCCCC	33.21	29978859
208	Phosphorylation	PPQPNDLYKNPTSSS CCCCCCCCCCCCCHH	16.16	29978859
209	Ubiquitination	PQPNDLYKNPTSSSE CCCCCCCCCCCCHHH	64.84	23503661
212	Phosphorylation	NDLYKNPTSSSEFYK CCCCCCCCCHHHHHH	51.11	29978859
213	O-linked_Glycosylation	DLYKNPTSSSEFYKA CCCCCCCCHHHHHHH	32.88	28657654
213	Phosphorylation	DLYKNPTSSSEFYKA CCCCCCCCHHHHHHH	32.88	29978859
214	Phosphorylation	LYKNPTSSSEFYKAQ CCCCCCCHHHHHHHC	36.04	29978859
215	Phosphorylation	YKNPTSSSEFYKAQG CCCCCCHHHHHHHCC	31.34	29978859
218	Phosphorylation	PTSSSEFYKAQGPLP CCCHHHHHHHCCCCC	11.02	29978859
219	Ubiquitination	TSSSEFYKAQGPLPN CCHHHHHHHCCCCCC	39.28	23000965
219 (in isoform 1)	Ubiquitination	-	39.28	21890473
229	Phosphorylation	GPLPNQHSLKGMEHR CCCCCCCCCCCCCCC	23.24	30266825
231	Ubiquitination	LPNQHSLKGMEHRGP CCCCCCCCCCCCCCC	60.26	32015554
236	Methylation	SLKGMEHRGPPPEYP CCCCCCCCCCCCCCC	46.11	-
263	Phosphorylation	PQEPGHFYSEHRLNQ CCCCCCCCCCCCCCC	13.89	29978859
264	Phosphorylation	QEPGHFYSEHRLNQP CCCCCCCCCCCCCCC	26.44	29978859
271	Ubiquitination	SEHRLNQPGRTEGQL CCCCCCCCCCCCCCC	32.91	32015554
280	Methylation	RTEGQLMRYQHPPEY CCCCCCCCCCCCCCC	36.23	-
281	Phosphorylation	TEGQLMRYQHPPEYG CCCCCCCCCCCCCCC	9.37	29978859
287	Phosphorylation	RYQHPPEYGAARPAQ CCCCCCCCCCCCCCC	20.17	29978859
291	Methylation	PPEYGAARPAQDISL CCCCCCCCCCCCCCC	26.93	-
297	Phosphorylation	ARPAQDISLPLSARN CCCCCCCCCCCCCCC	32.02	29449344
301	Phosphorylation	QDISLPLSARNSQPH CCCCCCCCCCCCCCC	24.20	29978859
305	Phosphorylation	LPLSARNSQPHSPTS CCCCCCCCCCCCCCC	39.26	17525332
309	Phosphorylation	ARNSQPHSPTSSLTS CCCCCCCCCCCCCCC	36.23	9533343
311	Phosphorylation	NSQPHSPTSSLTSGG CCCCCCCCCCCCCCC	33.68	30631047
312	Phosphorylation	SQPHSPTSSLTSGGS CCCCCCCCCCCCCCC	27.08	17525332
313	Phosphorylation	QPHSPTSSLTSGGSL CCCCCCCCCCCCCCC	37.84	28450419
315	Phosphorylation	HSPTSSLTSGGSLPL CCCCCCCCCCCCCCC	27.55	28450419
316	Phosphorylation	SPTSSLTSGGSLPLL CCCCCCCCCCCCCCC	46.58	28450419
319	Phosphorylation	SSLTSGGSLPLLQSP CCCCCCCCCCCCCCC	30.27	28450419
325	Phosphorylation	GSLPLLQSPPSTRLS CCCCCCCCCCCCCCC	38.45	29666759
328	Phosphorylation	PLLQSPPSTRLSPAR CCCCCCCCCCCCCCC	29.55	29978859
329	Phosphorylation	LLQSPPSTRLSPARH CCCCCCCCCCCCCCC	41.21	29978859
330	Ubiquitination	LQSPPSTRLSPARHP CCCCCCCCCCCCCCC	37.19	32015554
332	Phosphorylation	SPPSTRLSPARHPLV CCCCCCCCCCCCCCC	17.14	29978859
335	Methylation	STRLSPARHPLVPNQ CCCCCCCCCCCCCCC	35.03	-
367	Phosphorylation	QAHQGDHYRLSQPGL CCCCCCCHHCCCCCC	20.28	29978859
412	Methylation	EAYSAMPRAQPSSAS HHHHCCCCCCCCCCC	32.54	-
416	Phosphorylation	AMPRAQPSSASYQPV CCCCCCCCCCCCCCC	26.84	29978859
417	Phosphorylation	MPRAQPSSASYQPVP CCCCCCCCCCCCCCC	28.11	29978859
419	Phosphorylation	RAQPSSASYQPVPAD CCCCCCCCCCCCCCC	26.67	29978859
420	Phosphorylation	AQPSSASYQPVPADP CCCCCCCCCCCCCCH	19.29	29978859
442	Phosphorylation	QQMVEILSDENRNLR HHHHHHHCCCCHHHH	48.84	29978859
464	Ubiquitination	EKVARLQKVETEIQR HHHHHHHHHHHHHHH	46.78	32015554
464 (in isoform 1)	Ubiquitination	-	46.78	21890473
481	Ubiquitination	EAYENLVKSSSKREA HHHHHHHHCCHHHHH	48.03	32015554
496	Ubiquitination	LEKAMRNKLEGEIRR HHHHHHHHHHHHHHH	37.23	32015554
520	Ubiquitination	ERLETANKQLAEKEY HHHHHHHHHHHHHHH	44.20	32015554
527	Phosphorylation	KQLAEKEYEGSEDTR HHHHHHHHCCCHHHH	36.34	29978859
530	Phosphorylation	AEKEYEGSEDTRKTI HHHHHCCCHHHHHHH	21.99	28509920
536	Phosphorylation	GSEDTRKTISQLFAK CCHHHHHHHHHHHHH	23.67	113179225
538	Phosphorylation	EDTRKTISQLFAKNK HHHHHHHHHHHHHCH	26.51	28270605
543	Ubiquitination	TISQLFAKNKESQRE HHHHHHHHCHHHHHH	62.31	32015554
545	Acetylation	SQLFAKNKESQREKE HHHHHHCHHHHHHHH	59.02	20167786
553	Ubiquitination	ESQREKEKLEAELAT HHHHHHHHHHHHHHH	63.80	29967540
575	Methylation	QRRHIEIRDQALSNA HHHHHHHHHHHHHHH	19.73	-
585	Ubiquitination	ALSNAQAKVVKLEEE HHHHHHHHHHHHHHH	35.17	32015554
594	Sumoylation	VKLEEELKKKQVYVD HHHHHHHHHCCEEHH	62.29	-
594	Sumoylation	VKLEEELKKKQVYVD HHHHHHHHHCCEEHH	62.29	25218447
595	Sumoylation	KLEEELKKKQVYVDK HHHHHHHHCCEEHHH	62.15	-
595	Sumoylation	KLEEELKKKQVYVDK HHHHHHHHCCEEHHH	62.15	25218447
599	Phosphorylation	ELKKKQVYVDKVEKM HHHHCCEEHHHHHHH	10.63	2026007
605	Ubiquitination	VYVDKVEKMQQALVQ EEHHHHHHHHHHHHH	45.02	32015554
617	Glutathionylation	LVQLQAACEKREQLE HHHHHHHHHHHHHHH	7.69	22555962
647	Glutathionylation	IQQRQGNCQPTNVSE HHHHCCCCCCCCHHH	7.01	22555962
680	Ubiquitination	ALEADMTKWEQKYLE HHHCCCHHHHHHHHH	41.94	32015554
685	Phosphorylation	MTKWEQKYLEENVMR CHHHHHHHHHHHHHH	21.02	29978859
708	Phosphorylation	TVAAQRDTTVISHSP HHHHHCCCEEEECCC	25.75	28450419
709	Phosphorylation	VAAQRDTTVISHSPN HHHHCCCEEEECCCC	21.82	30177828
712	Phosphorylation	QRDTTVISHSPNTSY HCCCEEEECCCCCCH	17.36	30266825
714	Phosphorylation	DTTVISHSPNTSYDT CCEEEECCCCCCHHH	17.04	30266825
717	Phosphorylation	VISHSPNTSYDTALE EEECCCCCCHHHHHH	31.86	23911959
718	Phosphorylation	ISHSPNTSYDTALEA EECCCCCCHHHHHHH	27.87	28348404
719	Phosphorylation	SHSPNTSYDTALEAR ECCCCCCHHHHHHHH	18.44	19413330
721	Phosphorylation	SPNTSYDTALEARIQ CCCCCHHHHHHHHHH	25.55	28796482
739	Ubiquitination	EEILMANKRCLDMEG HHHHHHCHHHHCHHC	34.64	32015554
750	Phosphorylation	DMEGRIKTLHAQIIE CHHCCHHHHHHHHHH	22.77	113179223
758	Ubiquitination	LHAQIIEKDAMIKVL HHHHHHHHHHHHHHH	40.14	-
776	O-linked_Glycosylation	SRKEPSKTEQLSCMR CCCCCCHHHHHHCCC	33.05	28657654
776	Phosphorylation	SRKEPSKTEQLSCMR CCCCCCHHHHHHCCC	33.05	28509920
787	Phosphorylation	SCMRPAKSLMSISNA HCCCHHHHHHHHHCC	31.26	23401153
790	Phosphorylation	RPAKSLMSISNAGSG CHHHHHHHHHCCCCC	28.32	23401153
792	Phosphorylation	AKSLMSISNAGSGLL HHHHHHHHCCCCCHH	17.20	23401153
796	Phosphorylation	MSISNAGSGLLSHSS HHHHCCCCCHHCCCC	24.69	29978859
800	Phosphorylation	NAGSGLLSHSSTLTG CCCCCHHCCCCCCCC	26.77	23401153
802	Phosphorylation	GSGLLSHSSTLTGSP CCCHHCCCCCCCCCC	22.95	29978859
803	Phosphorylation	SGLLSHSSTLTGSPI CCHHCCCCCCCCCCC	23.24	29978859
804	Phosphorylation	GLLSHSSTLTGSPIM CHHCCCCCCCCCCCC	31.21	29978859
806	Phosphorylation	LSHSSTLTGSPIMEE HCCCCCCCCCCCCCC	35.38	29978859
808	Phosphorylation	HSSTLTGSPIMEEKR CCCCCCCCCCCCCCC	13.15	29978859
819	Phosphorylation	EEKRDDKSWKGSLGI CCCCCCCCCCCCCHH	40.80	23898821
823	Phosphorylation	DDKSWKGSLGILLGG CCCCCCCCCHHHCCC	21.50	25850435
832	Phosphorylation	GILLGGDYRAEYVPS HHHCCCCCCCEECCC	18.26	27642862
836	Phosphorylation	GGDYRAEYVPSTPSP CCCCCCEECCCCCCC	19.37	29978859
839	Phosphorylation	YRAEYVPSTPSPVPP CCCEECCCCCCCCCC	42.79	20363803
840	Phosphorylation	RAEYVPSTPSPVPPS CCEECCCCCCCCCCC	23.01	29978859
842	Phosphorylation	EYVPSTPSPVPPSTP EECCCCCCCCCCCCC	38.32	20363803
847	Phosphorylation	TPSPVPPSTPLLSAH CCCCCCCCCCCCCCC	36.27	29978859
848	Phosphorylation	PSPVPPSTPLLSAHS CCCCCCCCCCCCCCC	24.59	29978859
852	Phosphorylation	PPSTPLLSAHSKTGS CCCCCCCCCCCCCCC	31.45	29978859
855	Phosphorylation	TPLLSAHSKTGSRDC CCCCCCCCCCCCCCC	31.46	29978859
857	Phosphorylation	LLSAHSKTGSRDCST CCCCCCCCCCCCCCC	43.32	28102081
859	Phosphorylation	SAHSKTGSRDCSTQT CCCCCCCCCCCCCCC	30.12	30257219
863	Phosphorylation	KTGSRDCSTQTERGT CCCCCCCCCCCCCCC	28.04	29449344
864	Phosphorylation	TGSRDCSTQTERGTE CCCCCCCCCCCCCCC	45.93	29449344
1041	Phosphorylation	GPGPHRLSIPSLTCN CCCCCCCCCCCEECC	32.20	29666759
1044	Phosphorylation	PHRLSIPSLTCNPDK CCCCCCCCEECCCCC	34.34	26270265
1046	Phosphorylation	RLSIPSLTCNPDKTD CCCCCCEECCCCCCC	17.99	26270265
1052	Phosphorylation	LTCNPDKTDGPVFHS EECCCCCCCCCCCCC	54.27	29978859
1059	Phosphorylation	TDGPVFHSNTLERKT CCCCCCCCCCCCCCC	21.75	29978859
1061	Phosphorylation	GPVFHSNTLERKTPI CCCCCCCCCCCCCCE	32.77	17287340
1082	Phosphorylation	PDAEMVEYLI----- CCHHHHHHHC-----	9.78	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
175	S	Phosphorylation	Kinase	LATS1	F1M2K4	PSP
175	S	Phosphorylation	Kinase	LATS1	O95835	PSP
175	S	Phosphorylation	Kinase	LATS2	Q9NRM7	PSP
536	T	Phosphorylation	Kinase	PRKCI	P41743	GPS
538	S	Phosphorylation	Kinase	PRKCI	P41743	GPS
750	T	Phosphorylation	Kinase	PRKCI	P41743	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4L	Q96PU5	PMID:22385262
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4	P46934	PMID:22385262
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:23564455

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DLG1_HUMAN	DLG1	physical	19615732
FOXK2_HUMAN	FOXK2	physical	19615732
MERL_HUMAN	NF2	physical	19615732
DYL1_HUMAN	DYNLL1	physical	19615732
MPDZ_HUMAN	MPDZ	physical	19615732
LIN7A_HUMAN	LIN7A	physical	19615732
BAG3_HUMAN	BAG3	physical	19615732
YAP1_HUMAN	YAP1	physical	19615732
NED4L_HUMAN	NEDD4L	physical	19615732
NIN_HUMAN	NIN	physical	19615732
UIMC1_HUMAN	UIMC1	physical	19615732
LIN7C_HUMAN	LIN7C	physical	19615732
MPP5_HUMAN	MPP5	physical	19615732
LONP2_HUMAN	LONP2	physical	19615732
SCLT1_HUMAN	SCLT1	physical	19615732
DYL2_HUMAN	DYNLL2	physical	19615732
MPP7_HUMAN	MPP7	physical	19615732
AMOL1_HUMAN	AMOTL1	physical	19615732
FOXK1_HUMAN	FOXK1	physical	19615732
UBP11_HUMAN	USP11	physical	19615732
NEDD4_HUMAN	NEDD4	physical	22385262
ITCH_HUMAN	ITCH	physical	22385262
YAP1_HUMAN	YAP1	physical	22385262
MPDZ_HUMAN	MPDZ	physical	16678097
INADL_HUMAN	INADL	physical	16678097
RHG17_HUMAN	ARHGAP17	physical	16678097
AMOT_HUMAN	AMOT	physical	16678097
AMOL2_HUMAN	AMOTL2	physical	16678097
MPP5_HUMAN	MPP5	physical	16678097
MPP7_HUMAN	MPP7	physical	16678097
A4_HUMAN	APP	physical	21832049
VASP_HUMAN	VASP	physical	22939629
ITCH_HUMAN	ITCH	physical	23564455
ALMS1_HUMAN	ALMS1	physical	24255178
AMOL1_HUMAN	AMOTL1	physical	24255178
AMOL2_HUMAN	AMOTL2	physical	24255178
ANR26_HUMAN	ANKRD26	physical	24255178
CLIP1_HUMAN	CLIP1	physical	24255178
CNTRB_HUMAN	CNTROB	physical	24255178
CTNB1_HUMAN	CTNNB1	physical	24255178
DYL1_HUMAN	DYNLL1	physical	24255178
NIPS2_HUMAN	GBAS	physical	24255178
INADL_HUMAN	INADL	physical	24255178
MPDZ_HUMAN	MPDZ	physical	24255178
MPP5_HUMAN	MPP5	physical	24255178
MPP7_HUMAN	MPP7	physical	24255178
NIPS1_HUMAN	NIPSNAP1	physical	24255178
OFD1_HUMAN	OFD1	physical	24255178
LIPA1_HUMAN	PPFIA1	physical	24255178
KPCI_HUMAN	PRKCI	physical	24255178
RAB35_HUMAN	RAB35	physical	24255178
RASF8_HUMAN	RASSF8	physical	24255178
MTCL1_HUMAN	MTCL1	physical	24255178
SPICE_HUMAN	SPICE1	physical	24255178
ASPP2_HUMAN	TP53BP2	physical	24255178
KIBRA_HUMAN	WWC1	physical	24255178
XPR1_HUMAN	XPR1	physical	24255178
ACTB_HUMAN	ACTB	physical	24225952
YAP1_HUMAN	YAP1	physical	24225952
YAP1_HUMAN	YAP1	physical	24106267
AMOT_HUMAN	AMOT	physical	25416956
LURA1_HUMAN	LURAP1	physical	25416956
MERL_HUMAN	NF2	physical	26045165
ACD11_HUMAN	ACAD11	physical	24366813
AMOL1_HUMAN	AMOTL1	physical	24366813
DYL1_HUMAN	DYNLL1	physical	24366813
DYL2_HUMAN	DYNLL2	physical	24366813
LATS1_HUMAN	LATS1	physical	24366813
LIN7C_HUMAN	LIN7C	physical	24366813
MERL_HUMAN	NF2	physical	24366813
RIF1_HUMAN	RIF1	physical	24366813
NED4L_HUMAN	NEDD4L	physical	25633977
GAG_HV1H2	gag	physical	25633977
USP9X_HUMAN	USP9X	physical	27462448
USP9X_HUMAN	USP9X	physical	28720576

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 AMOT_HUMAN

Related Literatures of Post-Translational Modification

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-714; THR-717 ANDTYR-719, AND MASS SPECTROMETRY.	19413330 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305 AND SER-312, ANDMASS SPECTROMETRY.	17525332 [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 THR-1061, AND MASSSPECTROMETRY.	17287340 [Abstract]