dbPTM

CSRP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CSRP1_MOUSE
UniProt AC	P97315
Protein Name	Cysteine and glycine-rich protein 1
Gene Name	Csrp1
Organism	Mus musculus (Mouse).
Sequence Length	193
Subcellular Localization	Nucleus .
Protein Description	Could play a role in neuronal development..
Protein Sequence	MPNWGGGKKCGVCQKTVYFAEEVQCEGNSFHKSCFLCMVCKKNLDSTTVAVHGEEIYCKSCYGKKYGPKGYGYGQGAGTLSTDKGESLGIKHEEAPGHRPTTNPNASKFAQKIGGSERCPRCSQAVYAAEKVIGAGKSWHKSCFRCAKCGKGLESTTLADKDGEIYCKGCYAKNFGPKGFGFGQGAGALVHSE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Acetylation	MPNWGGGKKCGVCQK CCCCCCCCCCCCCCC	48.44	7618943
25	S-nitrosocysteine	YFAEEVQCEGNSFHK EEEEEEEECCCCCCC	9.75	-
25	S-palmitoylation	YFAEEVQCEGNSFHK EEEEEEEECCCCCCC	9.75	28680068
25	S-nitrosylation	YFAEEVQCEGNSFHK EEEEEEEECCCCCCC	9.75	21278135
33	Phosphorylation	EGNSFHKSCFLCMVC CCCCCCCCEEEEHHC	11.09	29899451
58	S-nitrosocysteine	VHGEEIYCKSCYGKK ECCEEEEEEECCCCC	3.00	-
58	S-nitrosylation	VHGEEIYCKSCYGKK ECCEEEEEEECCCCC	3.00	21278135
59	Acetylation	HGEEIYCKSCYGKKY CCEEEEEEECCCCCC	26.96	22826441
71	Phosphorylation	KKYGPKGYGYGQGAG CCCCCCCCCCCCCCC	17.19	25195567
73	Phosphorylation	YGPKGYGYGQGAGTL CCCCCCCCCCCCCEE	9.59	25195567
79	Phosphorylation	GYGQGAGTLSTDKGE CCCCCCCEECCCCCC	19.59	25521595
81	Phosphorylation	GQGAGTLSTDKGESL CCCCCEECCCCCCCC	34.10	29550500
82	Phosphorylation	QGAGTLSTDKGESLG CCCCEECCCCCCCCC	44.86	22942356
84	Acetylation	AGTLSTDKGESLGIK CCEECCCCCCCCCCC	65.74	23806337
101	Phosphorylation	EAPGHRPTTNPNASK CCCCCCCCCCCCHHH	38.88	25521595
102	Phosphorylation	APGHRPTTNPNASKF CCCCCCCCCCCHHHH	51.89	29899451
108	Acetylation	TTNPNASKFAQKIGG CCCCCHHHHHHHHCC	42.16	23806337
112	Ubiquitination	NASKFAQKIGGSERC CHHHHHHHHCCCCCC	39.63	22790023
112	Acetylation	NASKFAQKIGGSERC CHHHHHHHHCCCCCC	39.63	23806337
122	S-nitrosylation	GSERCPRCSQAVYAA CCCCCCCHHHHHHHH	1.82	21278135
122	S-nitrosocysteine	GSERCPRCSQAVYAA CCCCCCCHHHHHHHH	1.82	-
127	Phosphorylation	PRCSQAVYAAEKVIG CCHHHHHHHHHHHHC	11.78	17203969
131	Acetylation	QAVYAAEKVIGAGKS HHHHHHHHHHCCCCC	34.13	23806337
137	Acetylation	EKVIGAGKSWHKSCF HHHHCCCCCHHHHHH	50.25	23806337
151	Acetylation	FRCAKCGKGLESTTL HHHHCCCCCCCCCCE	70.55	7668267
157	Phosphorylation	GKGLESTTLADKDGE CCCCCCCCEECCCCC	29.27	25521595
161	Acetylation	ESTTLADKDGEIYCK CCCCEECCCCCEEEC	63.12	23806337
167	S-nitrosocysteine	DKDGEIYCKGCYAKN CCCCCEEECCCEECC	3.62	-
167	S-nitrosylation	DKDGEIYCKGCYAKN CCCCCEEECCCEECC	3.62	22588120
192	Phosphorylation	GAGALVHSE------ CCCCCCCCC------	37.21	24925903

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
Oops, there are no upstream regulatory protein records of CSRP1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CSRP1_MOUSE !!

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 CSRP1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of CSRP1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of CSRP1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASSSPECTROMETRY.	17114649 [Abstract]
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-127, AND MASSSPECTROMETRY.	17203969 [Abstract]