dbPTM

BASP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BASP1_MOUSE
UniProt AC	Q91XV3
Protein Name	Brain acid soluble protein 1
Gene Name	Basp1
Organism	Mus musculus (Mouse).
Sequence Length	226
Subcellular Localization	Cell membrane Lipid-anchor. Cell projection, growth cone. Associated with the membranes of growth cones that form the tips of elongating axons.
Protein Description
Protein Sequence	MGGKLSKKKKGYNVNDEKAKDKDKKAEGAGTEEEGTPKESEPQAAADATEVKESTEEKPKDAADGEAKAEEKEADKAAAAKEEAPKAEPEKSEGAAEEQPEPAPAPEQEAAAPGPAAGGEAPKAGEASAESTGAADGAAPEEGEAKKTEAPAAAGPEAKSDAAPAASDSKPSSAEPAPSSKETPAASEAPSSAAKAPAPAAPAAAEPQAEAPAAAASSEQSVAVKE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Myristoylation	------MGGKLSKKK ------CCCCCCCCC	41.78	-
10	Ubiquitination	GKLSKKKKGYNVNDE CCCCCCCCCCCCCHH	75.42	27667366
12	Phosphorylation	LSKKKKGYNVNDEKA CCCCCCCCCCCHHHH	25.47	29514104
18	Ubiquitination	GYNVNDEKAKDKDKK CCCCCHHHHHHHHHH	64.70	27667366
18	Acetylation	GYNVNDEKAKDKDKK CCCCCHHHHHHHHHH	64.70	23806337
20	Ubiquitination	NVNDEKAKDKDKKAE CCCHHHHHHHHHHCC	76.11	-
25	Ubiquitination	KAKDKDKKAEGAGTE HHHHHHHHCCCCCCC	62.90	22790023
31	Phosphorylation	KKAEGAGTEEEGTPK HHCCCCCCCCCCCCC	39.42	25521595
36	Phosphorylation	AGTEEEGTPKESEPQ CCCCCCCCCCCCCCC	34.17	25521595
38	Ubiquitination	TEEEGTPKESEPQAA CCCCCCCCCCCCCHH	73.95	22790023
40	Phosphorylation	EEGTPKESEPQAAAD CCCCCCCCCCCHHHH	61.78	25521595
49	Phosphorylation	PQAAADATEVKESTE CCHHHHCHHHHHHHC	41.69	25619855
52	Ubiquitination	AADATEVKESTEEKP HHHCHHHHHHHCCCC	39.45	22790023
54	Phosphorylation	DATEVKESTEEKPKD HCHHHHHHHCCCCCC	35.09	25521595
55	Phosphorylation	ATEVKESTEEKPKDA CHHHHHHHCCCCCCC	49.62	23684622
58	Ubiquitination	VKESTEEKPKDAADG HHHHHCCCCCCCCCC	51.65	22790023
60	Ubiquitination	ESTEEKPKDAADGEA HHHCCCCCCCCCCHH	71.69	27667366
68	Ubiquitination	DAADGEAKAEEKEAD CCCCCHHHHHHHHHH	52.62	27667366
72	Ubiquitination	GEAKAEEKEADKAAA CHHHHHHHHHHHHHH	50.11	-
76	Ubiquitination	AEEKEADKAAAAKEE HHHHHHHHHHHHHHH	47.15	-
81	Ubiquitination	ADKAAAAKEEAPKAE HHHHHHHHHHCCCCC	51.89	22790023
86	Ubiquitination	AAKEEAPKAEPEKSE HHHHHCCCCCCCCCC	72.87	27667366
91	Ubiquitination	APKAEPEKSEGAAEE CCCCCCCCCCCCCCC	65.60	27667366
92	Phosphorylation	PKAEPEKSEGAAEEQ CCCCCCCCCCCCCCC	39.33	25521595
128	Phosphorylation	APKAGEASAESTGAA CCCCCCCCHHHCCCC	28.41	25521595
131	Phosphorylation	AGEASAESTGAADGA CCCCCHHHCCCCCCC	31.68	25521595
132	Phosphorylation	GEASAESTGAADGAA CCCCHHHCCCCCCCC	23.50	25521595
146	Ubiquitination	APEEGEAKKTEAPAA CCCCCCCCCCCCCHH	56.79	27667366
147	Ubiquitination	PEEGEAKKTEAPAAA CCCCCCCCCCCCHHC	59.66	22790023
159	Ubiquitination	AAAGPEAKSDAAPAA HHCCCCHHCCCCCCC	47.40	27667366
160	Phosphorylation	AAGPEAKSDAAPAAS HCCCCHHCCCCCCCC	39.26	25619855
167	Phosphorylation	SDAAPAASDSKPSSA CCCCCCCCCCCCCCC	44.52	25521595
169	Phosphorylation	AAPAASDSKPSSAEP CCCCCCCCCCCCCCC	43.93	25521595
169	O-linked_Glycosylation	AAPAASDSKPSSAEP CCCCCCCCCCCCCCC	43.93	22517741
170	Succinylation	APAASDSKPSSAEPA CCCCCCCCCCCCCCC	54.64	23806337
170	Acetylation	APAASDSKPSSAEPA CCCCCCCCCCCCCCC	54.64	23806337
170	Ubiquitination	APAASDSKPSSAEPA CCCCCCCCCCCCCCC	54.64	27667366
172	Phosphorylation	AASDSKPSSAEPAPS CCCCCCCCCCCCCCC	46.01	25521595
173	Phosphorylation	ASDSKPSSAEPAPSS CCCCCCCCCCCCCCC	45.22	25521595
179	Phosphorylation	SSAEPAPSSKETPAA CCCCCCCCCCCCCCH	57.03	25619855
180	Phosphorylation	SAEPAPSSKETPAAS CCCCCCCCCCCCCHH	33.19	25619855
181	Ubiquitination	AEPAPSSKETPAASE CCCCCCCCCCCCHHH	70.69	27667366
183	Phosphorylation	PAPSSKETPAASEAP CCCCCCCCCCHHHCC	23.20	25619855
187	Phosphorylation	SKETPAASEAPSSAA CCCCCCHHHCCCHHH	36.08	25619855
191	Phosphorylation	PAASEAPSSAAKAPA CCHHHCCCHHHCCCC	39.39	25619855
192	Phosphorylation	AASEAPSSAAKAPAP CHHHCCCHHHCCCCC	31.05	25521595
217	Phosphorylation	EAPAAAASSEQSVAV CCCHHHHCCCCCCCC	29.67	25619855
218	Phosphorylation	APAAAASSEQSVAVK CCHHHHCCCCCCCCC	34.62	25521595
221	Phosphorylation	AAASSEQSVAVKE-- HHHCCCCCCCCCC--	14.16	25619855
225	Ubiquitination	SEQSVAVKE------ CCCCCCCCC------	48.22	27667366

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 BASP1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BASP1_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 BASP1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of BASP1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of BASP1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND MASSSPECTROMETRY.	19144319 [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 THR-31; THR-36; SER-92;SER-128; SER-160; SER-167; SER-173 AND SER-218, AND MASS SPECTROMETRY.	17114649 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31 AND THR-36, AND MASSSPECTROMETRY.	17242355 [Abstract]