dbPTM

LASP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LASP1_MOUSE
UniProt AC	Q61792
Protein Name	LIM and SH3 domain protein 1
Gene Name	Lasp1
Organism	Mus musculus (Mouse).
Sequence Length	263
Subcellular Localization	Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Associated with the F-actin rich cortical cytoskeleton..
Protein Description	Plays an important role in the regulation of dynamic actin-based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation may also serve to regulate actin-associated ion transport activities, not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell types (By similarity)..
Protein Sequence	MNPNCARCGKIVYPTEKVNCLDKYWHKACFHCETCKMTLNMKNYKGYEKKPYCNAHYPKQSFTMVADTPENLRLKQQSELQSQVRYKEEFEKNKGKGFSVVADTPELQRIKKTQDQISNIKYHEEFEKSRMGPSGGEGVEPERREAQDSSSYRRPTEQQQPQPHHIPTSAPVYQQPQQQQMTSSYGGYKEPAAPVSIQRSAPGGGGKRYRAVYDYSAADEDEVSFQDGDTIVNVQQIDDGWMYGTVERTGDTGMLPANYVEAI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MNPNCARC -------CCCCCCCC	19.88	-
17	Ubiquitination	KIVYPTEKVNCLDKY CEECCCCCCCCHHHH	41.02	-
17	Malonylation	KIVYPTEKVNCLDKY CEECCCCCCCCHHHH	41.02	26320211
17	Acetylation	KIVYPTEKVNCLDKY CEECCCCCCCCHHHH	41.02	23236377
20	Glutathionylation	YPTEKVNCLDKYWHK CCCCCCCCHHHHHHH	6.11	24333276
23	Acetylation	EKVNCLDKYWHKACF CCCCCHHHHHHHHHH	36.97	21728379
24	Phosphorylation	KVNCLDKYWHKACFH CCCCHHHHHHHHHHC	16.65	22499769
27	Acetylation	CLDKYWHKACFHCET CHHHHHHHHHHCCCC	32.48	22826441
29	Glutathionylation	DKYWHKACFHCETCK HHHHHHHHHCCCCCC	2.60	24333276
32	Glutathionylation	WHKACFHCETCKMTL HHHHHHCCCCCCEEE	2.02	24333276
35	Glutathionylation	ACFHCETCKMTLNMK HHHCCCCCCEEECCC	1.01	24333276
38	Phosphorylation	HCETCKMTLNMKNYK CCCCCCEEECCCCCC	10.65	25521595
42	Acetylation	CKMTLNMKNYKGYEK CCEEECCCCCCCCCC	56.93	-
42	Malonylation	CKMTLNMKNYKGYEK CCEEECCCCCCCCCC	56.93	26320211
47	Phosphorylation	NMKNYKGYEKKPYCN CCCCCCCCCCCCCCC	22.03	29514104
50	Acetylation	NYKGYEKKPYCNAHY CCCCCCCCCCCCCCC	29.31	22826441
52	Phosphorylation	KGYEKKPYCNAHYPK CCCCCCCCCCCCCCC	13.76	29514104
53	S-nitrosylation	GYEKKPYCNAHYPKQ CCCCCCCCCCCCCCC	5.00	21278135
53	Glutathionylation	GYEKKPYCNAHYPKQ CCCCCCCCCCCCCCC	5.00	24333276
53	S-nitrosocysteine	GYEKKPYCNAHYPKQ CCCCCCCCCCCCCCC	5.00	-
57	Phosphorylation	KPYCNAHYPKQSFTM CCCCCCCCCCCCEEE	15.09	29514104
61	Phosphorylation	NAHYPKQSFTMVADT CCCCCCCCEEEEECC	28.89	27180971
63	Phosphorylation	HYPKQSFTMVADTPE CCCCCCEEEEECCHH	18.91	28507225
68	Phosphorylation	SFTMVADTPENLRLK CEEEEECCHHHHHHH	23.82	26239621
75	Ubiquitination	TPENLRLKQQSELQS CHHHHHHHHHHHHHH	39.60	-
75	Methylation	TPENLRLKQQSELQS CHHHHHHHHHHHHHH	39.60	-
75	Malonylation	TPENLRLKQQSELQS CHHHHHHHHHHHHHH	39.60	26320211
78	Phosphorylation	NLRLKQQSELQSQVR HHHHHHHHHHHHHHH	37.47	29514104
86	Phosphorylation	ELQSQVRYKEEFEKN HHHHHHHHHHHHHHH	24.72	25367039
96	Acetylation	EFEKNKGKGFSVVAD HHHHHCCCCEEEEEC	59.39	22826441
96	Malonylation	EFEKNKGKGFSVVAD HHHHHCCCCEEEEEC	59.39	26320211
96	Ubiquitination	EFEKNKGKGFSVVAD HHHHHCCCCEEEEEC	59.39	-
99	Phosphorylation	KNKGKGFSVVADTPE HHCCCCEEEEECCHH	25.09	27180971
104	Phosphorylation	GFSVVADTPELQRIK CEEEEECCHHHHHHH	14.66	25521595
112	Malonylation	PELQRIKKTQDQISN HHHHHHHHCHHHHHC	49.39	26320211
112	Succinylation	PELQRIKKTQDQISN HHHHHHHHCHHHHHC	49.39	23806337
112	Acetylation	PELQRIKKTQDQISN HHHHHHHHCHHHHHC	49.39	23806337
112	Succinylation	PELQRIKKTQDQISN HHHHHHHHCHHHHHC	49.39	-
118	Phosphorylation	KKTQDQISNIKYHEE HHCHHHHHCCHHHHH	27.20	29514104
121	Acetylation	QDQISNIKYHEEFEK HHHHHCCHHHHHHHH	44.82	21728379
121	Malonylation	QDQISNIKYHEEFEK HHHHHCCHHHHHHHH	44.82	26320211
122	Phosphorylation	DQISNIKYHEEFEKS HHHHCCHHHHHHHHH	15.63	29514104
128	Malonylation	KYHEEFEKSRMGPSG HHHHHHHHHHCCCCC	49.00	26320211
128	Ubiquitination	KYHEEFEKSRMGPSG HHHHHHHHHHCCCCC	49.00	-
134	Phosphorylation	EKSRMGPSGGEGVEP HHHHCCCCCCCCCCH	54.42	29899451
156	Phosphorylation	SSSYRRPTEQQQPQP CCCCCCCCCCCCCCC	44.61	22817900
168	Phosphorylation	PQPHHIPTSAPVYQQ CCCCCCCCCCCCCCC	36.60	25367039
169	Phosphorylation	QPHHIPTSAPVYQQP CCCCCCCCCCCCCCH	25.81	25367039
173	Phosphorylation	IPTSAPVYQQPQQQQ CCCCCCCCCCHHHHC	10.60	25263469
182	Phosphorylation	QPQQQQMTSSYGGYK CHHHHCCHHHCCCCC	15.35	25367039
183	Phosphorylation	PQQQQMTSSYGGYKE HHHHCCHHHCCCCCC	19.07	25367039
184	Phosphorylation	QQQQMTSSYGGYKEP HHHCCHHHCCCCCCC	20.73	27087446
185	Phosphorylation	QQQMTSSYGGYKEPA HHCCHHHCCCCCCCC	17.84	25367039
188	Phosphorylation	MTSSYGGYKEPAAPV CHHHCCCCCCCCCCC	14.07	25367039
196	Phosphorylation	KEPAAPVSIQRSAPG CCCCCCCEEEECCCC	16.37	25367039
207	Acetylation	SAPGGGGKRYRAVYD CCCCCCCCEEEEEEE	49.91	22362459
243	Phosphorylation	QIDDGWMYGTVERTG ECCCCEEEEEEEECC	11.79	-
245	Phosphorylation	DDGWMYGTVERTGDT CCCEEEEEEEECCCC	11.16	-
259	Phosphorylation	TGMLPANYVEAI--- CCCEEHHHEEEC---	11.19	25777480

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
61	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
61	S	Phosphorylation	Kinase	PKG-FAMILY	-	GPS
99	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
99	S	Phosphorylation	Kinase	PKG-FAMILY	-	GPS
156	T	Phosphorylation	Kinase	PRKACA	P05132	GPS
156	T	Phosphorylation	Kinase	PRKG1	P0C605	GPS
156	T	Phosphorylation	Kinase	PKG1 ISO2	P0C605-2	PSP
156	T	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
156	T	Phosphorylation	Kinase	PKG-FAMILY	-	GPS
156	T	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LASP1_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 LASP1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZYX_MOUSE	Zyx	physical	15465019
VASP_MOUSE	Vasp	physical	15465019
LPP_MOUSE	Lpp	physical	15465019

Drug and Disease Associations

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

Regulatory Network of LASP1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphorylation of mouse LASP-1 on threonine 156 by cAMP- and cGMP-dependent protein kinase."; Keicher C., Gambaryan S., Schulze E., Marcus K., Meyer H.E., Butt E.; Biochem. Biophys. Res. Commun. 324:308-316(2004). Cited for: PHOSPHORYLATION AT THR-156.	15465019 [Abstract]