dbPTM

MOES_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MOES_HUMAN
UniProt AC	P26038
Protein Name	Moesin {ECO:0000303\|PubMed:1924289}
Gene Name	MSN {ECO:0000312\|HGNC:HGNC:7373}
Organism	Homo sapiens (Human).
Sequence Length	577
Subcellular Localization	Cell membrane Peripheral membrane protein Cytoplasmic side . Cytoplasm, cytoskeleton . Apical cell membrane Peripheral membrane protein Cytoplasmic side . Cell projection, microvillus membrane Peripheral membrane protein Cytoplasmic side . Cel
Protein Description	Probably involved in connections of major cytoskeletal structures to the plasma membrane. May inhibit herpes simplex virus 1 infection at an early stage. Plays a role in regulating the proliferation, migration, and adhesion of human lymphoid cells and participates in immunologic synapse formation. [PubMed: 27405666]
Protein Sequence	MPKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFESM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Acetylation	-----MPKTISVRVT -----CCCEEEEEEE	58.13	27452117
3	Malonylation	-----MPKTISVRVT -----CCCEEEEEEE	58.13	26320211
3	Ubiquitination	-----MPKTISVRVT -----CCCEEEEEEE	58.13	-
4	Phosphorylation	----MPKTISVRVTT ----CCCEEEEEEEE	16.77	23312004
6	Phosphorylation	--MPKTISVRVTTMD --CCCEEEEEEEECC	14.76	21955146
12	Sulfoxidation	ISVRVTTMDAELEFA EEEEEEECCEEEEEE	3.16	30846556
35	Acetylation	QLFDQVVKTIGLREV HHHHHHHHHHCCCEE	35.25	19608861
35	Ubiquitination	QLFDQVVKTIGLREV HHHHHHHHHHCCCEE	35.25	21890473
52	Phosphorylation	FGLQYQDTKGFSTWL EEEEEECCCCHHHHH	19.97	24719451
56	Phosphorylation	YQDTKGFSTWLKLNK EECCCCHHHHHHHCC	27.60	23403867
57	Phosphorylation	QDTKGFSTWLKLNKK ECCCCHHHHHHHCCC	32.33	23403867
60	Acetylation	KGFSTWLKLNKKVTA CCHHHHHHHCCCCCH	41.39	25953088
60	Malonylation	KGFSTWLKLNKKVTA CCHHHHHHHCCCCCH	41.39	26320211
60	Ubiquitination	KGFSTWLKLNKKVTA CCHHHHHHHCCCCCH	41.39	-
64	Acetylation	TWLKLNKKVTAQDVR HHHHHCCCCCHHHHH	43.68	16916647
64	Ubiquitination	TWLKLNKKVTAQDVR HHHHHCCCCCHHHHH	43.68	-
66	Phosphorylation	LKLNKKVTAQDVRKE HHHCCCCCHHHHHHH	27.73	21406692
71	Methylation	KVTAQDVRKESPLLF CCCHHHHHHHCCCEE	45.36	115483605
72	Malonylation	VTAQDVRKESPLLFK CCHHHHHHHCCCEEE	63.49	26320211
72	Ubiquitination	VTAQDVRKESPLLFK CCHHHHHHHCCCEEE	63.49	21906983
74	Phosphorylation	AQDVRKESPLLFKFR HHHHHHHCCCEEEEE	24.71	30266825
79	Acetylation	KESPLLFKFRAKFYP HHCCCEEEEEECCCC	33.63	19608861
79	Malonylation	KESPLLFKFRAKFYP HHCCCEEEEEECCCC	33.63	26320211
79	Ubiquitination	KESPLLFKFRAKFYP HHCCCEEEEEECCCC	33.63	21890473
83	Acetylation	LLFKFRAKFYPEDVS CEEEEEECCCCCCCC	40.97	23954790
83	Malonylation	LLFKFRAKFYPEDVS CEEEEEECCCCCCCC	40.97	26320211
83	Succinylation	LLFKFRAKFYPEDVS CEEEEEECCCCCCCC	40.97	-
83	Succinylation	LLFKFRAKFYPEDVS CEEEEEECCCCCCCC	40.97	-
83	Ubiquitination	LLFKFRAKFYPEDVS CEEEEEECCCCCCCC	40.97	21890473
85	Nitration	FKFRAKFYPEDVSEE EEEEECCCCCCCCHH	12.66	-
90	Phosphorylation	KFYPEDVSEELIQDI CCCCCCCCHHHHHHH	37.36	30087585
98	Phosphorylation	EELIQDITQRLFFLQ HHHHHHHHHHHHHHH	18.87	-
107	Ubiquitination	RLFFLQVKEGILNDD HHHHHHHHCCCCCCC	36.94	-
116	Phosphorylation	GILNDDIYCPPETAV CCCCCCCCCCHHHHH	13.09	17360941
117	S-nitrosocysteine	ILNDDIYCPPETAVL CCCCCCCCCHHHHHH	4.65	-
117	Glutathionylation	ILNDDIYCPPETAVL CCCCCCCCCHHHHHH	4.65	22555962
117	S-nitrosylation	ILNDDIYCPPETAVL CCCCCCCCCHHHHHH	4.65	25417112
121	Phosphorylation	DIYCPPETAVLLASY CCCCCHHHHHHHHHH	28.04	28122231
127	Phosphorylation	ETAVLLASYAVQSKY HHHHHHHHHHHHHHH	17.37	21712546
132	Phosphorylation	LASYAVQSKYGDFNK HHHHHHHHHHCCCCH	22.65	21712546
133	Acetylation	ASYAVQSKYGDFNKE HHHHHHHHHCCCCHH	35.84	133123
134	Phosphorylation	SYAVQSKYGDFNKEV HHHHHHHHCCCCHHH	27.46	28152594
139	Acetylation	SKYGDFNKEVHKSGY HHHCCCCHHHHHCCC	62.19	19608861
139	Malonylation	SKYGDFNKEVHKSGY HHHCCCCHHHHHCCC	62.19	26320211
139	Ubiquitination	SKYGDFNKEVHKSGY HHHCCCCHHHHHCCC	62.19	19608861
143	Acetylation	DFNKEVHKSGYLAGD CCCHHHHHCCCCCCC	51.24	25953088
143	Ubiquitination	DFNKEVHKSGYLAGD CCCHHHHHCCCCCCC	51.24	-
144	Phosphorylation	FNKEVHKSGYLAGDK CCHHHHHCCCCCCCC	20.14	23403867
146	Phosphorylation	KEVHKSGYLAGDKLL HHHHHCCCCCCCCCC	10.64	23403867
151	Acetylation	SGYLAGDKLLPQRVL CCCCCCCCCCHHHHH	51.51	23954790
151	Malonylation	SGYLAGDKLLPQRVL CCCCCCCCCCHHHHH	51.51	26320211
151	Ubiquitination	SGYLAGDKLLPQRVL CCCCCCCCCCHHHHH	51.51	-
162	Acetylation	QRVLEQHKLNKDQWE HHHHHHHCCCHHHHH	54.15	23749302
162	Ubiquitination	QRVLEQHKLNKDQWE HHHHHHHCCCHHHHH	54.15	21906983
165	Acetylation	LEQHKLNKDQWEERI HHHHCCCHHHHHHHH	62.83	23749302
165	Succinylation	LEQHKLNKDQWEERI HHHHCCCHHHHHHHH	62.83	23954790
165	Ubiquitination	LEQHKLNKDQWEERI HHHHCCCHHHHHHHH	62.83	-
182	Sulfoxidation	WHEEHRGMLREDAVL HHHHHCCCCCHHHHH	3.00	28465586
191	Phosphorylation	REDAVLEYLKIAQDL CHHHHHHHHHHHHHH	14.77	-
200	Sulfoxidation	KIAQDLEMYGVNYFS HHHHHHHHHCCEEEE	4.60	30846556
205	Phosphorylation	LEMYGVNYFSIKNKK HHHHCCEEEEEECCC	9.04	-
207	Phosphorylation	MYGVNYFSIKNKKGS HHCCEEEEEECCCCC	23.46	28348404
209	Acetylation	GVNYFSIKNKKGSEL CCEEEEEECCCCCEE	62.61	25953088
209	Ubiquitination	GVNYFSIKNKKGSEL CCEEEEEECCCCCEE	62.61	21890473
211	Acetylation	NYFSIKNKKGSELWL EEEEEECCCCCEEEE	54.21	25953088
211	Ubiquitination	NYFSIKNKKGSELWL EEEEEECCCCCEEEE	54.21	-
212	Ubiquitination	YFSIKNKKGSELWLG EEEEECCCCCEEEEE	76.65	-
214	Phosphorylation	SIKNKKGSELWLGVD EEECCCCCEEEEEEC	38.09	28122231
228	Phosphorylation	DALGLNIYEQNDRLT CCCCCCCHHCCCCCC	15.47	-
237	Acetylation	QNDRLTPKIGFPWSE CCCCCCCCCCCCHHH	50.67	26051181
237	Ubiquitination	QNDRLTPKIGFPWSE CCCCCCCCCCCCHHH	50.67	21906983
243	Phosphorylation	PKIGFPWSEIRNISF CCCCCCHHHHCCCCC	24.31	27050516
249	Phosphorylation	WSEIRNISFNDKKFV HHHHCCCCCCCCEEE	22.88	30108239
253	Acetylation	RNISFNDKKFVIKPI CCCCCCCCEEEEEEC	49.57	19608861
253	Malonylation	RNISFNDKKFVIKPI CCCCCCCCEEEEEEC	49.57	26320211
253	Ubiquitination	RNISFNDKKFVIKPI CCCCCCCCEEEEEEC	49.57	21906983
254	Malonylation	NISFNDKKFVIKPID CCCCCCCEEEEEECC	47.96	26320211
254	Ubiquitination	NISFNDKKFVIKPID CCCCCCCEEEEEECC	47.96	-
258	Acetylation	NDKKFVIKPIDKKAP CCCEEEEEECCCCCC	30.53	19608861
258	Ubiquitination	NDKKFVIKPIDKKAP CCCEEEEEECCCCCC	30.53	19608861
262	Acetylation	FVIKPIDKKAPDFVF EEEEECCCCCCCCEE	52.10	1221628941
262	Malonylation	FVIKPIDKKAPDFVF EEEEECCCCCCCCEE	52.10	26320211
262	Sumoylation	FVIKPIDKKAPDFVF EEEEECCCCCCCCEE	52.10	-
262	Ubiquitination	FVIKPIDKKAPDFVF EEEEECCCCCCCCEE	52.10	21906983
263	Acetylation	VIKPIDKKAPDFVFY EEEECCCCCCCCEEE	62.49	19608861
263	Malonylation	VIKPIDKKAPDFVFY EEEECCCCCCCCEEE	62.49	26320211
263	Ubiquitination	VIKPIDKKAPDFVFY EEEECCCCCCCCEEE	62.49	19608861
270	Phosphorylation	KAPDFVFYAPRLRIN CCCCCEEEECCHHCC	15.47	27273156
273	Methylation	DFVFYAPRLRINKRI CCEEEECCHHCCHHH	28.55	-
291	Phosphorylation	CMGNHELYMRRRKPD HCCCHHHHHCCCCCC	5.89	28258704
296	Malonylation	ELYMRRRKPDTIEVQ HHHHCCCCCCCHHHH	45.49	26320211
296	Ubiquitination	ELYMRRRKPDTIEVQ HHHHCCCCCCCHHHH	45.49	21906983
299	Phosphorylation	MRRRKPDTIEVQQMK HCCCCCCCHHHHHHH	27.80	28985074
305	Sulfoxidation	DTIEVQQMKAQAREE CCHHHHHHHHHHHHH	1.86	30846556
306	Methylation	TIEVQQMKAQAREEK CHHHHHHHHHHHHHH	32.77	24212791
306	Ubiquitination	TIEVQQMKAQAREEK CHHHHHHHHHHHHHH	32.77	21906983
322	Sulfoxidation	QKQMERAMLENEKKK HHHHHHHHHHHHHHH	6.37	30846556
327	Acetylation	RAMLENEKKKREMAE HHHHHHHHHHHHHHH	75.16	23749302
327	Succinylation	RAMLENEKKKREMAE HHHHHHHHHHHHHHH	75.16	23954790
344	Acetylation	KEKIEREKEELMERL HHHHHHHHHHHHHHH	63.81	19608861
344	Malonylation	KEKIEREKEELMERL HHHHHHHHHHHHHHH	63.81	26320211
344	Ubiquitination	KEKIEREKEELMERL HHHHHHHHHHHHHHH	63.81	19608861
352	Ubiquitination	EELMERLKQIEEQTK HHHHHHHHHHHHHHH	56.29	21906983
360	Ubiquitination	QIEEQTKKAQQELEE HHHHHHHHHHHHHHH	55.61	-
380	Ubiquitination	LELEQERKRAQSEAE HHHHHHHHHHHHHHH	51.86	-
384	Phosphorylation	QERKRAQSEAEKLAK HHHHHHHHHHHHHHH	37.48	23911959
388	Acetylation	RAQSEAEKLAKERQE HHHHHHHHHHHHHHH	61.87	23749302
388	Ubiquitination	RAQSEAEKLAKERQE HHHHHHHHHHHHHHH	61.87	19608861
391	Ubiquitination	SEAEKLAKERQEAEE HHHHHHHHHHHHHHH	64.96	-
400	Acetylation	RQEAEEAKEALLQAS HHHHHHHHHHHHHHH	46.96	23749302
400	Malonylation	RQEAEEAKEALLQAS HHHHHHHHHHHHHHH	46.96	26320211
400	Ubiquitination	RQEAEEAKEALLQAS HHHHHHHHHHHHHHH	46.96	-
407	Phosphorylation	KEALLQASRDQKKTQ HHHHHHHHHHHHHHH	24.35	29255136
412	Ubiquitination	QASRDQKKTQEQLAL HHHHHHHHHHHHHHH	50.21	-
413	Phosphorylation	ASRDQKKTQEQLALE HHHHHHHHHHHHHHH	44.36	20860994
421	Sulfoxidation	QEQLALEMAELTARI HHHHHHHHHHHHHHH	3.50	21406390
425	Phosphorylation	ALEMAELTARISQLE HHHHHHHHHHHHHHH	12.85	20860994
429	Phosphorylation	AELTARISQLEMARQ HHHHHHHHHHHHHHH	24.14	30108239
433	Sulfoxidation	ARISQLEMARQKKES HHHHHHHHHHHHHHH	5.18	21406390
440	Phosphorylation	MARQKKESEAVEWQQ HHHHHHHHHHHHHHH	39.47	27251275
448	Acetylation	EAVEWQQKAQMVQED HHHHHHHHHHHHHHH	26.03	25953088
448	Ubiquitination	EAVEWQQKAQMVQED HHHHHHHHHHHHHHH	26.03	21906983
451	Sulfoxidation	EWQQKAQMVQEDLEK HHHHHHHHHHHHHHH	3.92	21406390
458	Acetylation	MVQEDLEKTRAELKT HHHHHHHHHHHHHHH	51.08	23236377
458	Ubiquitination	MVQEDLEKTRAELKT HHHHHHHHHHHHHHH	51.08	21906983
464	Ubiquitination	EKTRAELKTAMSTPH HHHHHHHHHHHCCCC	26.24	21906983
465	Phosphorylation	KTRAELKTAMSTPHV HHHHHHHHHHCCCCC	39.97	23401153
468	Phosphorylation	AELKTAMSTPHVAEP HHHHHHHCCCCCCCC	36.00	21712546
469	Phosphorylation	ELKTAMSTPHVAEPA HHHHHHCCCCCCCCC	12.34	21712546
491	Phosphorylation	DENGAEASADLRADA CCCCHHHHHHHHHHH	17.51	28985074
504	Phosphorylation	DAMAKDRSEEERTTE HHHHCCCCHHHHCCH	60.54	30576142
509	Phosphorylation	DRSEEERTTEAEKNE CCCHHHHCCHHHHHH	32.06	28270605
510	Phosphorylation	RSEEERTTEAEKNER CCHHHHCCHHHHHHH	39.14	28270605
520	Ubiquitination	EKNERVQKHLKALTS HHHHHHHHHHHHHHH	48.31	-
523	Malonylation	ERVQKHLKALTSELA HHHHHHHHHHHHHHH	40.86	26320211
523	Ubiquitination	ERVQKHLKALTSELA HHHHHHHHHHHHHHH	40.86	21890473
526	Phosphorylation	QKHLKALTSELANAR HHHHHHHHHHHHHCC	25.64	29255136
527	Phosphorylation	KHLKALTSELANARD HHHHHHHHHHHHCCH	31.31	29255136
536	Phosphorylation	LANARDESKKTANDM HHHCCHHHHHHHHHH	43.68	28348404
537	Ubiquitination	ANARDESKKTANDMI HHCCHHHHHHHHHHH	52.69	-
538	Ubiquitination	NARDESKKTANDMIH HCCHHHHHHHHHHHH	63.25	-
539	Phosphorylation	ARDESKKTANDMIHA CCHHHHHHHHHHHHH	34.14	28555341
543	Sulfoxidation	SKKTANDMIHAENMR HHHHHHHHHHHHHHH	2.13	21406390
549	Sulfoxidation	DMIHAENMRLGRDKY HHHHHHHHHCCHHHH	2.55	30846556
556	Phosphorylation	MRLGRDKYKTLRQIR HHCCHHHHHHHHHHH	17.31	28796482
558	Dephosphorylation	LGRDKYKTLRQIRQG CCHHHHHHHHHHHCC	24.88	10480873
558	Phosphorylation	LGRDKYKTLRQIRQG CCHHHHHHHHHHHCC	24.88	22167270
567	Phosphorylation	RQIRQGNTKQRIDEF HHHHCCCHHHCHHHH	35.06	9456324
576	Phosphorylation	QRIDEFESM------ HCHHHHHCC------	34.80	25159151
577	Sulfoxidation	RIDEFESM------- CHHHHHCC-------	5.11	28465586

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
66	T	Phosphorylation	Kinase	GRK5	P34947	PSP
558	T	Phosphorylation	Kinase	GRK2	P25098	PSP
558	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
558	T	Phosphorylation	Kinase	PRKCQ	Q04759	GPS
558	T	Phosphorylation	Kinase	LRRK2	Q5S007	PSP
558	T	Phosphorylation	Kinase	MAP3K8	P41279	GPS
558	T	Phosphorylation	Kinase	HGK	O95819	PSP
558	T	Phosphorylation	Kinase	ROCK1	Q13464	PSP
558	T	Phosphorylation	Kinase	ROCK2	O75116	Uniprot
558	T	Phosphorylation	Kinase	SRC	P05480	PSP
558	T	Phosphorylation	Kinase	LOK	O94804	PSP
558	T	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
558	T	Phosphorylation	Kinase	ROCK-SUBFAMILY	-	GPS
558	T	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
558	T	Phosphorylation	Kinase	ROCK_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF1	Q9HCE7	PMID:20804422

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
117	C	Oxidation	25417112
S-nitrosylation of Cys-117 is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) implicating the iNOS-S100A8/9 transnitrosylase complex.
117	C	S-nitrosylation	25417112
S-nitrosylation of Cys-117 is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) implicating the iNOS-S100A8/9 transnitrosylase complex.
558	T	Phosphorylation	10212266
Phosphorylation on Thr-558 by STK10 negatively regulates lymphocyte migration and polarization.
558	T	Phosphorylation	10212266
Phosphorylation on Thr-558 is crucial for the formation of microvilli-like structures.

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 MOES_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TSC1_HUMAN	TSC1	physical	12226091
BID_HUMAN	BID	physical	15659383
TR10B_HUMAN	TNFRSF10B	physical	15659383
EZRI_HUMAN	EZR	physical	15659383
FADD_HUMAN	FADD	physical	15659383
TNFL6_HUMAN	FASLG	physical	15659383
MK08_HUMAN	MAPK8	physical	15659383
CASPA_HUMAN	CASP10	physical	15659383
CASP8_HUMAN	CASP8	physical	15659383
TNR1A_HUMAN	TNFRSF1A	physical	15659383
MOES_HUMAN	MSN	physical	10847681
NCF1_HUMAN	NCF1	physical	11716484
NCF4_HUMAN	NCF4	physical	11716484
NHRF1_HUMAN	SLC9A3R1	physical	9430655
EZRI_HUMAN	EZR	physical	8248180
ISG15_HUMAN	ISG15	physical	16009940
TF3C4_HUMAN	GTF3C4	physical	22939629
SRCAP_HUMAN	SRCAP	physical	22939629
S10AG_HUMAN	S100A16	physical	22939629
ICAM1_HUMAN	ICAM1	physical	23463506
CD81_HUMAN	CD81	physical	23463506
VCAM1_HUMAN	VCAM1	physical	23463506
ICAM3_HUMAN	ICAM3	physical	23463506
IGSF8_HUMAN	IGSF8	physical	23463506
ASNS_HUMAN	ASNS	physical	22863883
CAN2_HUMAN	CAPN2	physical	22863883
DHX15_HUMAN	DHX15	physical	22863883
PSF3_HUMAN	GINS3	physical	22863883
GSHB_HUMAN	GSS	physical	22863883
GRP78_HUMAN	HSPA5	physical	22863883
NSF1C_HUMAN	NSFL1C	physical	22863883
LIS1_HUMAN	PAFAH1B1	physical	22863883
PA1B2_HUMAN	PAFAH1B2	physical	22863883
PAPS1_HUMAN	PAPSS1	physical	22863883
ODPA_HUMAN	PDHA1	physical	22863883
IPP2_HUMAN	PPP1R2	physical	22863883
GDS1_HUMAN	RAP1GDS1	physical	22863883
VPS11_HUMAN	VPS11	physical	21148287
THIM_HUMAN	ACAA2	physical	26344197
ALDR_HUMAN	AKR1B1	physical	26344197
GDIR1_HUMAN	ARHGDIA	physical	26344197
CALR_HUMAN	CALR	physical	26344197
CALU_HUMAN	CALU	physical	26344197
CD2AP_HUMAN	CD2AP	physical	26344197
CTNB1_HUMAN	CTNNB1	physical	26344197
IF5AL_HUMAN	EIF5AL1	physical	26344197
ENOA_HUMAN	ENO1	physical	26344197
ENOG_HUMAN	ENO2	physical	26344197
FABP5_HUMAN	FABP5	physical	26344197
FAXC_HUMAN	FAXC	physical	26344197
FKBP2_HUMAN	FKBP2	physical	26344197
ROA1_HUMAN	HNRNPA1	physical	26344197
HCD2_HUMAN	HSD17B10	physical	26344197
HSP74_HUMAN	HSPA4	physical	26344197
HS74L_HUMAN	HSPA4L	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
HS105_HUMAN	HSPH1	physical	26344197
INO1_HUMAN	ISYNA1	physical	26344197
PLAK_HUMAN	JUP	physical	26344197
PLSL_HUMAN	LCP1	physical	26344197
NOTC2_HUMAN	NOTCH2	physical	26344197
PDIA1_HUMAN	P4HB	physical	26344197
6PGD_HUMAN	PGD	physical	26344197
PGK1_HUMAN	PGK1	physical	26344197
PGK2_HUMAN	PGK2	physical	26344197
PLSI_HUMAN	PLS1	physical	26344197
PLST_HUMAN	PLS3	physical	26344197
RCN1_HUMAN	RCN1	physical	26344197
STIP1_HUMAN	STIP1	physical	26344197
TAGL2_HUMAN	TAGLN2	physical	26344197
TKT_HUMAN	TKT	physical	26344197
UCHL3_HUMAN	UCHL3	physical	26344197
WDR1_HUMAN	WDR1	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.

Regulatory Network of MOES_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-35; LYS-79; LYS-139 ANDLYS-388, AND MASS SPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64, AND MASS SPECTROMETRY.	16916647 [Abstract]
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 SER-576, AND MASSSPECTROMETRY.	18669648 [Abstract]
"LOK is a major ERM kinase in resting lymphocytes and regulatescytoskeletal rearrangement through ERM phosphorylation."; Belkina N.V., Liu Y., Hao J.J., Karasuyama H., Shaw S.; Proc. Natl. Acad. Sci. U.S.A. 106:4707-4712(2009). Cited for: PHOSPHORYLATION AT THR-558, AND MUTAGENESIS OF TYR-556 AND THR-558.	19255442 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-116, AND MASSSPECTROMETRY.	19690332 [Abstract]

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