dbPTM

MOES_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MOES_RAT
UniProt AC	O35763
Protein Name	Moesin {ECO:0000250\|UniProtKB:P26038}
Gene Name	Msn {ECO:0000312\|RGD:621260}
Organism	Rattus norvegicus (Rat).
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.; Probably involved in connections of major cytoskeletal structures to the plasma membrane. Plays a role in regulating the proliferation, migration, and adhesion of human lymphoid cells and participates in immunologic synapse formation..
Protein Sequence	MPKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKAFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQMERALLENEKKKRELAEKEKEKIEREKEELMEKLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLASEMAELTARVSQLEMARKKKESEAEECHQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEHDEQDENGAEASAELRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTTNDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFESM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
35	Acetylation	QLFDQVVKTIGLREV HHHHHHHHHHCCCEE	35.25	22902405
56	Phosphorylation	YQDTKAFSTWLKLNK ECCCCHHHHHHHHCC	24.43	22673903
57	Phosphorylation	QDTKAFSTWLKLNKK CCCCHHHHHHHHCCC	28.50	22673903
60	Acetylation	KAFSTWLKLNKKVTA CHHHHHHHHCCCCCH	41.39	22902405
74	Phosphorylation	AQDVRKESPLLFKFR HHHHHHHCCCEEEEE	24.71	23984901
79	Acetylation	KESPLLFKFRAKFYP HHCCCEEEEEECCCC	33.63	22902405
83	Acetylation	LLFKFRAKFYPEDVS CEEEEEECCCCCCCC	40.97	22902405
83	Succinylation	LLFKFRAKFYPEDVS CEEEEEECCCCCCCC	40.97	-
83	Succinylation	LLFKFRAKFYPEDVS CEEEEEECCCCCCCC	40.97	-
116	Phosphorylation	GILNDDIYCPPETAV CCCCCCCCCCHHHHH	13.09	-
117	S-nitrosocysteine	ILNDDIYCPPETAVL CCCCCCCCCHHHHHH	4.65	-
117	S-nitrosylation	ILNDDIYCPPETAVL CCCCCCCCCHHHHHH	4.65	-
139	Acetylation	SKYGDFNKEVHKSGY HHHCCCCHHHHHCCC	62.19	22902405
143	Acetylation	DFNKEVHKSGYLAGD CCCHHHHHCCCCCCC	51.24	22902405
151	Acetylation	SGYLAGDKLLPQRVL CCCCCCCCCCHHHHH	51.51	22902405
162	Ubiquitination	QRVLEQHKLNKDQWE HHHHHHHCCCHHHHH	54.15	-
162	Acetylation	QRVLEQHKLNKDQWE HHHHHHHCCCHHHHH	54.15	22902405
165	Acetylation	LEQHKLNKDQWEERI HHHHCCCHHHHHHHH	62.83	22902405
209	Acetylation	GVNYFSIKNKKGSEL CCEEEEEECCCCCEE	62.61	22902405
237	Acetylation	QNDRLTPKIGFPWSE CCCCCCCCCCCCHHH	50.67	22902405
243	Phosphorylation	PKIGFPWSEIRNISF CCCCCCHHHHCCCCC	24.31	22673903
249	Phosphorylation	WSEIRNISFNDKKFV HHHHCCCCCCCCEEE	22.88	22673903
253	Acetylation	RNISFNDKKFVIKPI CCCCCCCCEEEEEEC	49.57	22902405
254	Acetylation	NISFNDKKFVIKPID CCCCCCCEEEEEECC	47.96	22902405
258	Acetylation	NDKKFVIKPIDKKAP CCCEEEEEECCCCCC	30.53	22902405
258	Succinylation	NDKKFVIKPIDKKAP CCCEEEEEECCCCCC	30.53	26843850
262	Acetylation	FVIKPIDKKAPDFVF EEEEECCCCCCCCEE	52.10	22902405
263	Succinylation	VIKPIDKKAPDFVFY EEEECCCCCCCCEEE	62.49	26843850
270	Phosphorylation	KAPDFVFYAPRLRIN CCCCCEEEECCHHCC	15.47	-
327	Acetylation	RALLENEKKKRELAE HHHHHHHHHHHHHHH	75.16	22902405
335	Acetylation	KKRELAEKEKEKIER HHHHHHHHHHHHHHH	69.36	22902405
344	Acetylation	KEKIEREKEELMEKL HHHHHHHHHHHHHHH	63.81	22902405
350	Acetylation	EKEELMEKLKQIEEQ HHHHHHHHHHHHHHH	47.20	22902405
352	Acetylation	EELMEKLKQIEEQTK HHHHHHHHHHHHHHH	61.37	22902405
359	Acetylation	KQIEEQTKKAQQELE HHHHHHHHHHHHHHH	45.89	22902405
384	Phosphorylation	QERKRAQSEAEKLAK HHHHHHHHHHHHHHH	37.48	17089331
388	Acetylation	RAQSEAEKLAKERQE HHHHHHHHHHHHHHH	61.87	22902405
400	Acetylation	RQEAEEAKEALLQAS HHHHHHHHHHHHHHH	46.96	22902405
407	Phosphorylation	KEALLQASRDQKKTQ HHHHHHHHHHHHHHH	24.35	27097102
437	Acetylation	QLEMARKKKESEAEE HHHHHHHHHHHHHHH	57.11	22902405
459	Phosphorylation	VQEDLEKTRAELKTA HHHHHHHHHHHHHHH	26.24	22673903
465	Phosphorylation	KTRAELKTAMSTPHV HHHHHHHHHHCCCCC	39.97	30181290
468	Phosphorylation	AELKTAMSTPHVAEP HHHHHHHCCCCCCCC	36.00	30181290
469	Phosphorylation	ELKTAMSTPHVAEPA HHHHHHCCCCCCCCC	12.34	30181290
501	Acetylation	LRADAMAKDRSEEER HHHHHHHCCCCHHHH	40.36	22902405
523	Acetylation	ERVQKHLKALTSELA HHHHHHHHHHHHHHH	40.86	22902405
526	Phosphorylation	QKHLKALTSELANAR HHHHHHHHHHHHHCC	25.64	27097102
527	Phosphorylation	KHLKALTSELANARD HHHHHHHHHHHHCCH	31.31	27097102
537	Acetylation	ANARDESKKTTNDMI HHCCHHHCCCHHHHH	52.68	22902405
558	Phosphorylation	LGRDKYKTLRQIRQG CCHHHHHHHHHHHCC	24.88	16938849
576	Phosphorylation	QRIDEFESM------ HCHHHHHCC------	34.80	27097102

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
558	T	Phosphorylation	Kinase	MAP3K14	Q99558	GPS
558	T	Phosphorylation	Kinase	ROCK2	Q62868	Uniprot
558	T	Phosphorylation	Kinase	STK10	E9PTG8	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
117	C	Oxidation	-
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	-
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	-
Phosphorylation on Thr-558 by STK10 negatively regulates lymphocyte migration and polarization (By similarity).
558	T	Phosphorylation	-
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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of MOES_RAT !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MOES_RAT

Related Literatures of Post-Translational Modification

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