dbPTM

BASP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BASP1_HUMAN
UniProt AC	P80723
Protein Name	Brain acid soluble protein 1
Gene Name	BASP1
Organism	Homo sapiens (Human).
Sequence Length	227
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	MGGKLSKKKKGYNVNDEKAKEKDKKAEGAATEEEGTPKESEPQAAAEPAEAKEGKEKPDQDAEGKAEEKEGEKDAAAAKEEAPKAEPEKTEGAAEAKAEPPKAPEQEQAAPGPAAGGEAPKAAEAAAAPAESAAPAAGEEPSKEEGEPKKTEAPAAPAAQETKSDGAPASDSKPGSSEAAPSSKETPAATEAPSSTPKAQGPAASAEEPKPVEAPAANSDQTVTVKE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	N-myristoyl glycine	------MGGKLSKKK ------CCCCCCCCC	41.78	-
2	Myristoylation	------MGGKLSKKK ------CCCCCCCCC	41.78	9310187
10	Ubiquitination	GKLSKKKKGYNVNDE CCCCCCCCCCCCCHH	75.42	33845483
12	Phosphorylation	LSKKKKGYNVNDEKA CCCCCCCCCCCHHHH	25.47	-
18	Succinylation	GYNVNDEKAKEKDKK CCCCCHHHHHHHHHH	68.56	23954790
18	Acetylation	GYNVNDEKAKEKDKK CCCCCHHHHHHHHHH	68.56	27452117
18	2-Hydroxyisobutyrylation	GYNVNDEKAKEKDKK CCCCCHHHHHHHHHH	68.56	-
18	Ubiquitination	GYNVNDEKAKEKDKK CCCCCHHHHHHHHHH	68.56	21963094
20	Ubiquitination	NVNDEKAKEKDKKAE CCCHHHHHHHHHHHH	76.10	22817900
22	Ubiquitination	NDEKAKEKDKKAEGA CHHHHHHHHHHHHHC	74.31	22817900
24	Ubiquitination	EKAKEKDKKAEGAAT HHHHHHHHHHHHCCC	66.02	21963094
25	Sumoylation	KAKEKDKKAEGAATE HHHHHHHHHHHCCCC	62.90	28112733
25	Ubiquitination	KAKEKDKKAEGAATE HHHHHHHHHHHCCCC	62.90	33845483
31	Phosphorylation	KKAEGAATEEEGTPK HHHHHCCCCCCCCCC	43.31	22167270
36	Phosphorylation	AATEEEGTPKESEPQ CCCCCCCCCCCCCCC	34.17	22167270
38	Acetylation	TEEEGTPKESEPQAA CCCCCCCCCCCCCHH	73.95	26051181
38	Ubiquitination	TEEEGTPKESEPQAA CCCCCCCCCCCCCHH	73.95	21963094
40	Phosphorylation	EEGTPKESEPQAAAE CCCCCCCCCCCHHHC	61.78	25159151
52	Ubiquitination	AAEPAEAKEGKEKPD HHCHHHHHCCCCCCC	59.51	21963094
52	Acetylation	AAEPAEAKEGKEKPD HHCHHHHHCCCCCCC	59.51	26051181
55	Ubiquitination	PAEAKEGKEKPDQDA HHHHHCCCCCCCCCC	64.75	22817900
57	Ubiquitination	EAKEGKEKPDQDAEG HHHCCCCCCCCCCCC	58.33	32142685
65	Ubiquitination	PDQDAEGKAEEKEGE CCCCCCCHHHHHHHH	44.10	33845483
69	Ubiquitination	AEGKAEEKEGEKDAA CCCHHHHHHHHHHHH	63.63	30230243
73	Succinylation	AEEKEGEKDAAAAKE HHHHHHHHHHHHHHH	64.62	23954790
73	Ubiquitination	AEEKEGEKDAAAAKE HHHHHHHHHHHHHHH	64.62	33845483
79	Ubiquitination	EKDAAAAKEEAPKAE HHHHHHHHHHCCCCC	51.89	21963094
79	Succinylation	EKDAAAAKEEAPKAE HHHHHHHHHHCCCCC	51.89	23954790
84	Ubiquitination	AAKEEAPKAEPEKTE HHHHHCCCCCCCCCC	72.87	22817900
84	Acetylation	AAKEEAPKAEPEKTE HHHHHCCCCCCCCCC	72.87	26051181
84	Succinylation	AAKEEAPKAEPEKTE HHHHHCCCCCCCCCC	72.87	23954790
84	Sumoylation	AAKEEAPKAEPEKTE HHHHHCCCCCCCCCC	72.87	28112733
89	Ubiquitination	APKAEPEKTEGAAEA CCCCCCCCCCCHHHH	63.69	21963094
89	Acetylation	APKAEPEKTEGAAEA CCCCCCCCCCCHHHH	63.69	26051181
90	Phosphorylation	PKAEPEKTEGAAEAK CCCCCCCCCCHHHHH	37.68	21601212
97	Ubiquitination	TEGAAEAKAEPPKAP CCCHHHHHCCCCCCC	44.80	21963094
97	Acetylation	TEGAAEAKAEPPKAP CCCHHHHHCCCCCCC	44.80	26051181
97	Sumoylation	TEGAAEAKAEPPKAP CCCHHHHHCCCCCCC	44.80	28112733
102	Ubiquitination	EAKAEPPKAPEQEQA HHHCCCCCCCHHHHC	83.64	22817900
102	Acetylation	EAKAEPPKAPEQEQA HHHCCCCCCCHHHHC	83.64	26051181
121	Ubiquitination	AAGGEAPKAAEAAAA CCCCCCCHHHHHHCC	68.24	33845483
132	Phosphorylation	AAAAPAESAAPAAGE HHCCCHHHCCCCCCC	31.66	23663014
142	Phosphorylation	PAAGEEPSKEEGEPK CCCCCCCCCCCCCCC	56.85	25159151
143	Ubiquitination	AAGEEPSKEEGEPKK CCCCCCCCCCCCCCC	71.19	21963094
143	Succinylation	AAGEEPSKEEGEPKK CCCCCCCCCCCCCCC	71.19	23954790
143	Sumoylation	AAGEEPSKEEGEPKK CCCCCCCCCCCCCCC	71.19	-
143	Acetylation	AAGEEPSKEEGEPKK CCCCCCCCCCCCCCC	71.19	26051181
149	Ubiquitination	SKEEGEPKKTEAPAA CCCCCCCCCCCCCCC	68.94	23503661
150	Ubiquitination	KEEGEPKKTEAPAAP CCCCCCCCCCCCCCC	63.41	33845483
150	Acetylation	KEEGEPKKTEAPAAP CCCCCCCCCCCCCCC	63.41	26051181
151	Phosphorylation	EEGEPKKTEAPAAPA CCCCCCCCCCCCCCC	43.43	23403867
151	O-linked_Glycosylation	EEGEPKKTEAPAAPA CCCCCCCCCCCCCCC	43.43	28657654
162	Phosphorylation	AAPAAQETKSDGAPA CCCCHHHHCCCCCCC	24.62	23927012
163	Ubiquitination	APAAQETKSDGAPAS CCCHHHHCCCCCCCC	45.88	21963094
163	Sumoylation	APAAQETKSDGAPAS CCCHHHHCCCCCCCC	45.88	25114211
163	Acetylation	APAAQETKSDGAPAS CCCHHHHCCCCCCCC	45.88	26051181
164	Phosphorylation	PAAQETKSDGAPASD CCHHHHCCCCCCCCC	49.01	22167270
170	Phosphorylation	KSDGAPASDSKPGSS CCCCCCCCCCCCCCC	41.16	22167270
172	Phosphorylation	DGAPASDSKPGSSEA CCCCCCCCCCCCCCC	37.95	23927012
173	Acetylation	GAPASDSKPGSSEAA CCCCCCCCCCCCCCC	59.39	26051181
173	Ubiquitination	GAPASDSKPGSSEAA CCCCCCCCCCCCCCC	59.39	21963094
176	Phosphorylation	ASDSKPGSSEAAPSS CCCCCCCCCCCCCCC	33.27	25159151
177	Phosphorylation	SDSKPGSSEAAPSSK CCCCCCCCCCCCCCC	36.85	23927012
182	Phosphorylation	GSSEAAPSSKETPAA CCCCCCCCCCCCCCC	49.68	23927012
183	Phosphorylation	SSEAAPSSKETPAAT CCCCCCCCCCCCCCC	33.19	25159151
184	Acetylation	SEAAPSSKETPAATE CCCCCCCCCCCCCCC	70.69	26051181
184	Ubiquitination	SEAAPSSKETPAATE CCCCCCCCCCCCCCC	70.69	21963094
186	Phosphorylation	AAPSSKETPAATEAP CCCCCCCCCCCCCCC	23.20	25159151
190	O-linked_Glycosylation	SKETPAATEAPSSTP CCCCCCCCCCCCCCC	34.48	28657654
190	Phosphorylation	SKETPAATEAPSSTP CCCCCCCCCCCCCCC	34.48	21712546
194	Phosphorylation	PAATEAPSSTPKAQG CCCCCCCCCCCCCCC	54.62	22167270
195	Phosphorylation	AATEAPSSTPKAQGP CCCCCCCCCCCCCCC	47.90	22167270
196	Phosphorylation	ATEAPSSTPKAQGPA CCCCCCCCCCCCCCC	32.90	19664994
198	Ubiquitination	EAPSSTPKAQGPAAS CCCCCCCCCCCCCCC	54.13	21963094
205	Phosphorylation	KAQGPAASAEEPKPV CCCCCCCCCCCCCCC	38.02	25159151
210	Ubiquitination	AASAEEPKPVEAPAA CCCCCCCCCCCCCCC	66.04	23503661
210	Acetylation	AASAEEPKPVEAPAA CCCCCCCCCCCCCCC	66.04	26051181
219	Phosphorylation	VEAPAANSDQTVTVK CCCCCCCCCCCEEEC	26.77	9310187
222	Phosphorylation	PAANSDQTVTVKE-- CCCCCCCCEEECC--	24.12	22167270
224	Phosphorylation	ANSDQTVTVKE---- CCCCCCEEECC----	29.28	23663014
226	Ubiquitination	SDQTVTVKE------ CCCCEEECC------	48.63	21963094

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_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BASP1_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 BASP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
U5S1_HUMAN	EFTUD2	physical	22939629
GRP78_HUMAN	HSPA5	physical	22939629
QOR_HUMAN	CRYZ	physical	22863883
HMGN5_HUMAN	HMGN5	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 BASP1_HUMAN

Related Literatures of Post-Translational Modification

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 THR-31; THR-36; SER-164;SER-170; SER-172; SER-176; THR-196 AND SER-205, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36; SER-164 AND THR-196,AND MASS SPECTROMETRY.	17081983 [Abstract]
"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 THR-196, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-196, AND MASSSPECTROMETRY.	17924679 [Abstract]