dbPTM

LASP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LASP1_HUMAN
UniProt AC	Q14847
Protein Name	LIM and SH3 domain protein 1
Gene Name	LASP1
Organism	Homo sapiens (Human).
Sequence Length	261
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	MNPNCARCGKIVYPTEKVNCLDKFWHKACFHCETCKMTLNMKNYKGYEKKPYCNAHYPKQSFTMVADTPENLRLKQQSELQSQVRYKEEFEKNKGKGFSVVADTPELQRIKKTQDQISNIKYHEEFEKSRMGPSGGEGMEPERRDSQDGSSYRRPLEQQQPHHIPTSAPVYQQPQQQPVAQSYGGYKEPAAPVSIQRSAPGGGGKRYRAVYDYSAADEDEVSFQDGDTIVNVQQIDDGWMYGTVERTGDTGMLPANYVEAI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MNPNCARC -------CCCCCCCC	19.88	12665801
10	Ubiquitination	PNCARCGKIVYPTEK CCCCCCCCEECCCCC	32.40	-
10 (in isoform 2)	Ubiquitination	-	32.40	-
13	Phosphorylation	ARCGKIVYPTEKVNC CCCCCEECCCCCCCC	14.12	28152594
15	Phosphorylation	CGKIVYPTEKVNCLD CCCEECCCCCCCCHH	30.65	28152594
17	Acetylation	KIVYPTEKVNCLDKF CEECCCCCCCCHHHH	41.02	23954790
17	Malonylation	KIVYPTEKVNCLDKF CEECCCCCCCCHHHH	41.02	26320211
17	Ubiquitination	KIVYPTEKVNCLDKF CEECCCCCCCCHHHH	41.02	-
17 (in isoform 2)	Ubiquitination	-	41.02	-
23	Acetylation	EKVNCLDKFWHKACF CCCCCHHHHHHHHHH	37.09	25825284
23	Ubiquitination	EKVNCLDKFWHKACF CCCCCHHHHHHHHHH	37.09	21890473
23 (in isoform 1)	Ubiquitination	-	37.09	21890473
23 (in isoform 2)	Ubiquitination	-	37.09	21890473
27	Acetylation	CLDKFWHKACFHCET CHHHHHHHHHHCCCC	37.13	26051181
31	Ubiquitination	FWHKACFHCETCKMT HHHHHHHCCCCCCEE	14.37	-
34	Phosphorylation	KACFHCETCKMTLNM HHHHCCCCCCEEECC	23.87	28258704
36	Acetylation	CFHCETCKMTLNMKN HHCCCCCCEEECCCC	42.19	26051181
38	Phosphorylation	HCETCKMTLNMKNYK CCCCCCEEECCCCCC	10.65	23403867
40	Ubiquitination	ETCKMTLNMKNYKGY CCCCEEECCCCCCCC	30.16	21890473
42	Acetylation	CKMTLNMKNYKGYEK CCEEECCCCCCCCCC	56.93	19608861
42	Malonylation	CKMTLNMKNYKGYEK CCEEECCCCCCCCCC	56.93	26320211
42	Ubiquitination	CKMTLNMKNYKGYEK CCEEECCCCCCCCCC	56.93	21906983
42 (in isoform 1)	Ubiquitination	-	56.93	21890473
42 (in isoform 2)	Ubiquitination	-	56.93	21890473
44	Phosphorylation	MTLNMKNYKGYEKKP EEECCCCCCCCCCCC	10.56	20068231
45	Succinylation	TLNMKNYKGYEKKPY EECCCCCCCCCCCCC	65.49	23954790
45	Ubiquitination	TLNMKNYKGYEKKPY EECCCCCCCCCCCCC	65.49	-
47	Phosphorylation	NMKNYKGYEKKPYCN CCCCCCCCCCCCCCC	22.03	-
49	Acetylation	KNYKGYEKKPYCNAH CCCCCCCCCCCCCCC	51.03	26051181
50	Acetylation	NYKGYEKKPYCNAHY CCCCCCCCCCCCCCC	29.31	26822725
50	Ubiquitination	NYKGYEKKPYCNAHY CCCCCCCCCCCCCCC	29.31	-
52	Phosphorylation	KGYEKKPYCNAHYPK CCCCCCCCCCCCCCC	13.76	28152594
57	Phosphorylation	KPYCNAHYPKQSFTM CCCCCCCCCCCCEEE	15.09	28152594
59	Acetylation	YCNAHYPKQSFTMVA CCCCCCCCCCEEEEE	51.94	26051181
59	Malonylation	YCNAHYPKQSFTMVA CCCCCCCCCCEEEEE	51.94	26320211
59	Ubiquitination	YCNAHYPKQSFTMVA CCCCCCCCCCEEEEE	51.94	-
59 (in isoform 2)	Ubiquitination	-	51.94	-
61	Phosphorylation	NAHYPKQSFTMVADT CCCCCCCCEEEEECC	28.89	30266825
63	Phosphorylation	HYPKQSFTMVADTPE CCCCCCEEEEECCHH	18.91	30266825
64	Sulfoxidation	YPKQSFTMVADTPEN CCCCCEEEEECCHHH	1.89	21406390
65	Acetylation	PKQSFTMVADTPENL CCCCEEEEECCHHHH	3.86	-
65	Ubiquitination	PKQSFTMVADTPENL CCCCEEEEECCHHHH	3.86	21890473
68	Phosphorylation	SFTMVADTPENLRLK CEEEEECCHHHHHHH	23.82	29255136
72	Ubiquitination	VADTPENLRLKQQSE EECCHHHHHHHHHHH	6.91	-
75	Sumoylation	TPENLRLKQQSELQS CHHHHHHHHHHHHHH	39.60	-
75	Malonylation	TPENLRLKQQSELQS CHHHHHHHHHHHHHH	39.60	26320211
75	Methylation	TPENLRLKQQSELQS CHHHHHHHHHHHHHH	39.60	24129315
75	Sumoylation	TPENLRLKQQSELQS CHHHHHHHHHHHHHH	39.60	-
75	Ubiquitination	TPENLRLKQQSELQS CHHHHHHHHHHHHHH	39.60	-
75 (in isoform 1)	Ubiquitination	-	39.60	21890473
75 (in isoform 2)	Ubiquitination	-	39.60	21890473
78	Phosphorylation	NLRLKQQSELQSQVR HHHHHHHHHHHHHHH	37.47	21406692
82	Phosphorylation	KQQSELQSQVRYKEE HHHHHHHHHHHHHHH	43.18	25159151
86	Phosphorylation	ELQSQVRYKEEFEKN HHHHHHHHHHHHHHH	24.72	21406692
87	Sumoylation	LQSQVRYKEEFEKNK HHHHHHHHHHHHHHC	39.96	-
87	Sumoylation	LQSQVRYKEEFEKNK HHHHHHHHHHHHHHC	39.96	-
87	Ubiquitination	LQSQVRYKEEFEKNK HHHHHHHHHHHHHHC	39.96	-
92	Acetylation	RYKEEFEKNKGKGFS HHHHHHHHHCCCCEE	70.09	30583743
92	Methylation	RYKEEFEKNKGKGFS HHHHHHHHHCCCCEE	70.09	30583743
96	Acetylation	EFEKNKGKGFSVVAD HHHHHCCCCEEEEEC	59.39	26051181
96	Malonylation	EFEKNKGKGFSVVAD HHHHHCCCCEEEEEC	59.39	26320211
96	Ubiquitination	EFEKNKGKGFSVVAD HHHHHCCCCEEEEEC	59.39	-
96 (in isoform 1)	Ubiquitination	-	59.39	21890473
96 (in isoform 2)	Ubiquitination	-	59.39	21890473
99	Phosphorylation	KNKGKGFSVVADTPE HHCCCCEEEEECCHH	25.09	29255136
104	Phosphorylation	GFSVVADTPELQRIK CEEEEECCHHHHHHH	14.66	19664994
112	Succinylation	PELQRIKKTQDQISN HHHHHHHHCHHHHHC	49.39	-
112	Succinylation	PELQRIKKTQDQISN HHHHHHHHCHHHHHC	49.39	-
112	Ubiquitination	PELQRIKKTQDQISN HHHHHHHHCHHHHHC	49.39	-
113	Phosphorylation	ELQRIKKTQDQISNI HHHHHHHCHHHHHCC	32.17	23312004
118	Phosphorylation	KKTQDQISNIKYHEE HHCHHHHHCCHHHHH	27.20	25159151
121	Acetylation	QDQISNIKYHEEFEK HHHHHCCHHHHHHHH	44.82	23954790
121	Ubiquitination	QDQISNIKYHEEFEK HHHHHCCHHHHHHHH	44.82	21890473
121 (in isoform 1)	Ubiquitination	-	44.82	21890473
121 (in isoform 2)	Ubiquitination	-	44.82	21890473
122	Phosphorylation	DQISNIKYHEEFEKS HHHHCCHHHHHHHHH	15.63	28102081
128	Acetylation	KYHEEFEKSRMGPSG HHHHHHHHHHCCCCC	49.00	19608861
128	Methylation	KYHEEFEKSRMGPSG HHHHHHHHHHCCCCC	49.00	22640041
128	Ubiquitination	KYHEEFEKSRMGPSG HHHHHHHHHHCCCCC	49.00	-
129	Phosphorylation	YHEEFEKSRMGPSGG HHHHHHHHHCCCCCC	21.94	28857561
131	Acetylation	EEFEKSRMGPSGGEG HHHHHHHCCCCCCCC	13.78	-
134	Phosphorylation	EKSRMGPSGGEGMEP HHHHCCCCCCCCCCC	54.42	23927012
146	Phosphorylation	MEPERRDSQDGSSYR CCCCCCCCCCCCCCC	28.49	29255136
150	Phosphorylation	RRDSQDGSSYRRPLE CCCCCCCCCCCCCHH	32.27	22167270
151	Phosphorylation	RDSQDGSSYRRPLEQ CCCCCCCCCCCCHHH	28.34	21945579
152	Phosphorylation	DSQDGSSYRRPLEQQ CCCCCCCCCCCHHHC	16.61	21945579
166	O-linked_Glycosylation	QQPHHIPTSAPVYQQ CCCCCCCCCCCCCCC	36.60	OGP
166	Phosphorylation	QQPHHIPTSAPVYQQ CCCCCCCCCCCCCCC	36.60	21945579
167	Phosphorylation	QPHHIPTSAPVYQQP CCCCCCCCCCCCCCC	25.81	21945579
171	Phosphorylation	IPTSAPVYQQPQQQP CCCCCCCCCCCCCCC	10.60	21945579
182	Phosphorylation	QQQPVAQSYGGYKEP CCCCCHHHCCCCCCC	18.92	21945579
183	Phosphorylation	QQPVAQSYGGYKEPA CCCCHHHCCCCCCCC	11.50	21945579
186	Phosphorylation	VAQSYGGYKEPAAPV CHHHCCCCCCCCCCC	14.07	21945579
187	Acetylation	AQSYGGYKEPAAPVS HHHCCCCCCCCCCCE	61.57	23236377
187	Ubiquitination	AQSYGGYKEPAAPVS HHHCCCCCCCCCCCE	61.57	-
194	Phosphorylation	KEPAAPVSIQRSAPG CCCCCCCEEEECCCC	16.37	26356563
198	Phosphorylation	APVSIQRSAPGGGGK CCCEEEECCCCCCCC	23.57	25159151
205	Acetylation	SAPGGGGKRYRAVYD CCCCCCCCEEEEEEE	49.91	22362455
241	Phosphorylation	QIDDGWMYGTVERTG ECCCCEEEEEEEECC	11.79	-
247	Phosphorylation	MYGTVERTGDTGMLP EEEEEEECCCCCCEE	26.38	22617229
252	Sulfoxidation	ERTGDTGMLPANYVE EECCCCCCEEHHHEE	4.38	30846556
257	Nitration	TGMLPANYVEAI--- CCCEEHHHEEEC---	11.19	-
257	Phosphorylation	TGMLPANYVEAI--- CCCEEHHHEEEC---	11.19	27642862

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
146	S	Phosphorylation	Kinase	CDK7	P50613	PhosphoELM
146	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
146	S	Phosphorylation	Kinase	PRKG1	Q13976	GPS
146	S	Phosphorylation	Kinase	PKG1 ISO2	Q13976-2	PSP
146	S	Phosphorylation	Kinase	PRKG2	Q13237	GPS
146	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
146	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
171	Y	Phosphorylation	Kinase	BCR-ABL1	A9UF07	PSP
171	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
171	Y	Phosphorylation	Kinase	LYN	P07948	PSP
171	Y	Phosphorylation	Kinase	SRC	P00523	PSP
171	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LASP1_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 LASP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PCH2_HUMAN	TRIP13	physical	16189514
PLS1_HUMAN	PLSCR1	physical	16189514
MDFI_HUMAN	MDFI	physical	16189514
PCH2_HUMAN	TRIP13	physical	19060904
MDFI_HUMAN	MDFI	physical	19060904
DAZP2_HUMAN	DAZAP2	physical	19060904
PSA3_HUMAN	PSMA3	physical	25416956
REL_HUMAN	REL	physical	25416956
TRI27_HUMAN	TRIM27	physical	25416956
ITF2_HUMAN	TCF4	physical	25416956
PCH2_HUMAN	TRIP13	physical	25416956
FXR2_HUMAN	FXR2	physical	25416956
SPY2_HUMAN	SPRY2	physical	25416956
ARHGF_HUMAN	ARHGEF15	physical	25416956
ZC21A_HUMAN	ZC2HC1A	physical	25416956
THAP1_HUMAN	THAP1	physical	25416956
SEPT3_HUMAN	SEPT3	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
RHXF2_HUMAN	RHOXF2	physical	25416956
KRA42_HUMAN	KRTAP4-2	physical	25416956
ZBTB9_HUMAN	ZBTB9	physical	25416956
AHNK_HUMAN	AHNAK	physical	26344197
ARFG1_HUMAN	ARFGAP1	physical	26344197
DDB1_HUMAN	DDB1	physical	26344197
IF4B_HUMAN	EIF4B	physical	26344197
HSPB1_HUMAN	HSPB1	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
LEG1_HUMAN	LGALS1	physical	26344197
MAP4_HUMAN	MAP4	physical	26344197
NXF1_HUMAN	NXF1	physical	26344197
PCH2_HUMAN	TRIP13	physical	21516116
PGK1_HUMAN	PGK1	physical	25982273
EZRI_HUMAN	EZR	physical	25982273
SPTN1_HUMAN	SPTAN1	physical	25982273
NUCL_HUMAN	NCL	physical	25982273
UHRF1_HUMAN	UHRF1	physical	25982273
NAT10_HUMAN	NAT10	physical	25982273
PDIA5_HUMAN	PDIA5	physical	25982273
API5_HUMAN	API5	physical	25982273
K1C18_HUMAN	KRT18	physical	25982273
K22E_HUMAN	KRT2	physical	25982273
G3BP2_HUMAN	G3BP2	physical	25982273
AP3M1_HUMAN	AP3M1	physical	25982273
NCOR2_HUMAN	NCOR2	physical	25982273
CDK12_HUMAN	CDK12	physical	25982273
MYO1C_HUMAN	MYO1C	physical	25982273
ARP3_HUMAN	ACTR3	physical	25982273
CLH1_HUMAN	CLTC	physical	25982273
DNMT1_HUMAN	DNMT1	physical	25982273
EHMT2_HUMAN	EHMT2	physical	25982273
SNAI1_HUMAN	SNAI1	physical	25982273
H31_HUMAN	HIST1H3A	physical	25982273

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 LASP1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-104, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides."; Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.; Nat. Biotechnol. 21:566-569(2003). Cited for: PROTEIN SEQUENCE OF 1-7, AND ACETYLATION AT MET-1.	12665801 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42 AND LYS-128, AND MASSSPECTROMETRY.	19608861 [Abstract]
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-68; THR-104 AND SER-146,AND MASS SPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND MASSSPECTROMETRY.	18088087 [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-68; THR-104 AND SER-151,AND MASS SPECTROMETRY.	17924679 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68 AND THR-104, AND MASSSPECTROMETRY.	19690332 [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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-104, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-171, AND MASSSPECTROMETRY.	16094384 [Abstract]