dbPTM

PLSL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PLSL_HUMAN
UniProt AC	P13796
Protein Name	Plastin-2
Gene Name	LCP1
Organism	Homo sapiens (Human).
Sequence Length	627
Subcellular Localization	Cytoplasm, cytoskeleton . Cell junction . Cell projection . Cell projection, ruffle membrane Peripheral membrane protein Cytoplasmic side . Relocalizes to the immunological synapse between peripheral blood T-lymphocytes and antibody-presenting ce
Protein Description	Actin-binding protein. [PubMed: 16636079]
Protein Sequence	MARGSVSDEEMMELREAFAKVDTDGNGYISFNELNDLFKAACLPLPGYRVREITENLMATGDLDQDGRISFDEFIKIFHGLKSTDVAKTFRKAINKKEGICAIGGTSEQSSVGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTNDLFNAVGDGIVLCKMINLSVPDTIDERTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIELSRNEALIALLREGESLEDLMKLSPEELLLRWANYHLENAGCNKIGNFSTDIKDSKAYYHLLEQVAPKGDEEGVPAVVIDMSGLREKDDIQRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNRYPALHKPENQDIDWGALEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGGNMKKLENCNYAVELGKNQAKFSLVGIGGQDLNEGNRTLTLALIWQLMRRYTLNILEEIGGGQKVNDDIIVNWVNETLREAKKSSSISSFKDPKISTSLPVLDLIDAIQPGSINYDLLKTENLNDDEKLNNAKYAISMARKIGARVYALPEDLVEVNPKMVMTVFACLMGKGMKRV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MARGSVSDE ------CCCCCCCHH	25.25	-
5	Phosphorylation	---MARGSVSDEEMM ---CCCCCCCHHHHH	16.94	28176443
7	Phosphorylation	-MARGSVSDEEMMEL -CCCCCCCHHHHHHH	40.79	23401153
11	Sulfoxidation	GSVSDEEMMELREAF CCCCHHHHHHHHHHH	2.08	21406390
20	Acetylation	ELREAFAKVDTDGNG HHHHHHHHCCCCCCC	33.90	133035
20	Ubiquitination	ELREAFAKVDTDGNG HHHHHHHHCCCCCCC	33.90	-
23	Phosphorylation	EAFAKVDTDGNGYIS HHHHHCCCCCCCEEE	49.12	28796482
28	Phosphorylation	VDTDGNGYISFNELN CCCCCCCEEEHHHHH	9.44	27155012
30	Phosphorylation	TDGNGYISFNELNDL CCCCCEEEHHHHHHH	17.34	28450419
39	Ubiquitination	NELNDLFKAACLPLP HHHHHHHHHHHCCCC	42.23	-
41	Acetylation	LNDLFKAACLPLPGY HHHHHHHHHCCCCCC	8.93	-
41	Ubiquitination	LNDLFKAACLPLPGY HHHHHHHHHCCCCCC	8.93	-
48	Phosphorylation	ACLPLPGYRVREITE HHCCCCCCCHHHHHH	12.19	23917254
54	Phosphorylation	GYRVREITENLMATG CCCHHHHHHHHHHCC	17.67	-
58	Sulfoxidation	REITENLMATGDLDQ HHHHHHHHHCCCCCC	4.77	21406390
76	Acetylation	ISFDEFIKIFHGLKS CCHHHHHHHHHCCCC	44.64	19608861
76	Ubiquitination	ISFDEFIKIFHGLKS CCHHHHHHHHHCCCC	44.64	21906983
82	Acetylation	IKIFHGLKSTDVAKT HHHHHCCCCHHHHHH	56.77	23749302
82	Ubiquitination	IKIFHGLKSTDVAKT HHHHHCCCCHHHHHH	56.77	21890473
83	Phosphorylation	KIFHGLKSTDVAKTF HHHHCCCCHHHHHHH	34.58	30108239
84	Phosphorylation	IFHGLKSTDVAKTFR HHHCCCCHHHHHHHH	32.67	30108239
88	Acetylation	LKSTDVAKTFRKAIN CCCHHHHHHHHHHHH	48.31	19608861
88	Ubiquitination	LKSTDVAKTFRKAIN CCCHHHHHHHHHHHH	48.31	21906983
89	Phosphorylation	KSTDVAKTFRKAINK CCHHHHHHHHHHHHH	20.95	28122231
97	Ubiquitination	FRKAINKKEGICAIG HHHHHHHCCCEEEEC	57.60	21890473
106	O-linked_Glycosylation	GICAIGGTSEQSSVG CEEEECCCCCCCCCC	24.71	32870666
106	Phosphorylation	GICAIGGTSEQSSVG CEEEECCCCCCCCCC	24.71	30576142
107	Phosphorylation	ICAIGGTSEQSSVGT EEEECCCCCCCCCCC	36.59	28450419
110	Phosphorylation	IGGTSEQSSVGTQHS ECCCCCCCCCCCCCC	23.96	28450419
111	Acetylation	GGTSEQSSVGTQHSY CCCCCCCCCCCCCCC	25.02	-
111	Ubiquitination	GGTSEQSSVGTQHSY CCCCCCCCCCCCCCC	25.02	-
111	O-linked_Glycosylation	GGTSEQSSVGTQHSY CCCCCCCCCCCCCCC	25.02	32870666
111	Phosphorylation	GGTSEQSSVGTQHSY CCCCCCCCCCCCCCC	25.02	28450419
114	Phosphorylation	SEQSSVGTQHSYSEE CCCCCCCCCCCCCHH	22.43	28450419
117	Phosphorylation	SSVGTQHSYSEEEKY CCCCCCCCCCHHHHH	22.12	23401153
118	Phosphorylation	SVGTQHSYSEEEKYA CCCCCCCCCHHHHHH	20.27	28450419
119	O-linked_Glycosylation	VGTQHSYSEEEKYAF CCCCCCCCHHHHHHH	41.36	32870666
119	Phosphorylation	VGTQHSYSEEEKYAF CCCCCCCCHHHHHHH	41.36	28450419
123	Ubiquitination	HSYSEEEKYAFVNWI CCCCHHHHHHHHHHH	45.20	-
124	Phosphorylation	SYSEEEKYAFVNWIN CCCHHHHHHHHHHHH	14.46	25159151
132	Ubiquitination	AFVNWINKALENDPD HHHHHHHHHHHCCCC	45.26	21890473
140	Glutathionylation	ALENDPDCRHVIPMN HHHCCCCCCCCCCCC	3.84	22555962
148	Acetylation	RHVIPMNPNTNDLFN CCCCCCCCCCHHHHH	42.65	-
148	Ubiquitination	RHVIPMNPNTNDLFN CCCCCCCCCCHHHHH	42.65	-
153	Ubiquitination	MNPNTNDLFNAVGDG CCCCCHHHHHHHCCC	3.75	21890473
164	S-palmitoylation	VGDGIVLCKMINLSV HCCCHHEEEECCCCC	1.62	29575903
165	Ubiquitination	GDGIVLCKMINLSVP CCCHHEEEECCCCCC	38.36	21890473
166	Sulfoxidation	DGIVLCKMINLSVPD CCHHEEEECCCCCCC	2.10	21406390
170	Phosphorylation	LCKMINLSVPDTIDE EEEECCCCCCCCCCC	27.41	21712546
179	Ubiquitination	PDTIDERTINKKKLT CCCCCCCCCCCCCCC	27.18	-
200	Phosphorylation	NLNLALNSASAIGCH HHHHHHHHCCCCCCE	25.17	18452278
202	Phosphorylation	NLALNSASAIGCHVV HHHHHHCCCCCCEEE	21.90	18452278
243	Phosphorylation	LFADIELSRNEALIA HHCCCEECCCHHHHH	21.92	20068231
257	Phosphorylation	ALLREGESLEDLMKL HHHHCCCCHHHHHHC	48.17	23401153
262	Sulfoxidation	GESLEDLMKLSPEEL CCCHHHHHHCCHHHH	6.76	28465586
263	Acetylation	ESLEDLMKLSPEELL CCHHHHHHCCHHHHH	53.78	26822725
263	Ubiquitination	ESLEDLMKLSPEELL CCHHHHHHCCHHHHH	53.78	-
265	Phosphorylation	LEDLMKLSPEELLLR HHHHHHCCHHHHHHH	25.42	21815630
276	Phosphorylation	LLLRWANYHLENAGC HHHHHHHHHHHHCCC	10.47	27155012
285	Ubiquitination	LENAGCNKIGNFSTD HHHCCCCCCCCCCCC	56.94	21890473
290	Phosphorylation	CNKIGNFSTDIKDSK CCCCCCCCCCCCCCH	29.21	23401153
291	Phosphorylation	NKIGNFSTDIKDSKA CCCCCCCCCCCCCHH	37.29	22617229
294	Acetylation	GNFSTDIKDSKAYYH CCCCCCCCCCHHHHH	59.78	19608861
294	Ubiquitination	GNFSTDIKDSKAYYH CCCCCCCCCCHHHHH	59.78	19608861
296	Phosphorylation	FSTDIKDSKAYYHLL CCCCCCCCHHHHHHH	17.74	21949786
297	Acetylation	STDIKDSKAYYHLLE CCCCCCCHHHHHHHH	51.01	19608861
297	Ubiquitination	STDIKDSKAYYHLLE CCCCCCCHHHHHHHH	51.01	21906983
299	Phosphorylation	DIKDSKAYYHLLEQV CCCCCHHHHHHHHHH	8.64	28796482
300	Phosphorylation	IKDSKAYYHLLEQVA CCCCHHHHHHHHHHC	7.28	28796482
322	Sulfoxidation	VPAVVIDMSGLREKD CCEEEEECCCCCCHH	2.05	21406390
323	Phosphorylation	PAVVIDMSGLREKDD CEEEEECCCCCCHHH	30.81	30576142
337	Sulfoxidation	DIQRAECMLQQAERL HHHHHHHHHHHHHHH	2.59	21406390
351	Phosphorylation	LGCRQFVTATDVVRG HCCCCEEEHHHHHCC	25.73	29978859
353	Phosphorylation	CRQFVTATDVVRGNP CCCEEEHHHHHCCCC	21.69	28464451
361	Acetylation	DVVRGNPKLNLAFIA HHHCCCCCCCHHHHH	54.74	19608861
361	Ubiquitination	DVVRGNPKLNLAFIA HHHCCCCCCCHHHHH	54.74	19608861
374	Phosphorylation	IANLFNRYPALHKPE HHHHHHHCCCCCCCC	8.25	27155012
379	Acetylation	NRYPALHKPENQDID HHCCCCCCCCCCCCC	55.68	25953088
379	Ubiquitination	NRYPALHKPENQDID HHCCCCCCCCCCCCC	55.68	-
399	Phosphorylation	GETREERTFRNWMNS CCCHHHHHHHHHHHH	30.17	-
406	Phosphorylation	TFRNWMNSLGVNPRV HHHHHHHHCCCCCCH	15.47	23401153
417	Phosphorylation	NPRVNHLYSDLSDAL CCCHHHHHCCHHHHH	7.81	26356563
418	Phosphorylation	PRVNHLYSDLSDALV CCHHHHHCCHHHHHH	38.13	26356563
430	Phosphorylation	ALVIFQLYEKIKVPV HHHHHHHHHHCCCCC	12.37	22817900
432	Ubiquitination	VIFQLYEKIKVPVDW HHHHHHHHCCCCCCH	33.98	-
434	Acetylation	FQLYEKIKVPVDWNR HHHHHHCCCCCCHHH	52.10	25953088
434	Methylation	FQLYEKIKVPVDWNR HHHHHHCCCCCCHHH	52.10	30783021
434	Ubiquitination	FQLYEKIKVPVDWNR HHHHHHCCCCCCHHH	52.10	-
444	Acetylation	VDWNRVNKPPYPKLG CCHHHCCCCCCCCCC	44.50	26822725
444	Methylation	VDWNRVNKPPYPKLG CCHHHCCCCCCCCCC	44.50	116252109
444	Ubiquitination	VDWNRVNKPPYPKLG CCHHHCCCCCCCCCC	44.50	-
449	Acetylation	VNKPPYPKLGGNMKK CCCCCCCCCCCCHHH	54.65	25953088
449	Ubiquitination	VNKPPYPKLGGNMKK CCCCCCCCCCCCHHH	54.65	-
455	Acetylation	PKLGGNMKKLENCNY CCCCCCHHHHCCCCC	59.20	25953088
456	Acetylation	KLGGNMKKLENCNYA CCCCCHHHHCCCCCE	50.71	25953088
456	Ubiquitination	KLGGNMKKLENCNYA CCCCCHHHHCCCCCE	50.71	-
468	Acetylation	NYAVELGKNQAKFSL CCEEEECCCCEEEEE	59.52	25953088
468	Ubiquitination	NYAVELGKNQAKFSL CCEEEECCCCEEEEE	59.52	19608861
472	Acetylation	ELGKNQAKFSLVGIG EECCCCEEEEEEEEC	26.23	19608861
472	Ubiquitination	ELGKNQAKFSLVGIG EECCCCEEEEEEEEC	26.23	19608861
474	Phosphorylation	GKNQAKFSLVGIGGQ CCCCEEEEEEEECCC	22.80	23401153
502	Phosphorylation	IWQLMRRYTLNILEE HHHHHHHHHHHHHHH	12.76	21406692
503	Phosphorylation	WQLMRRYTLNILEEI HHHHHHHHHHHHHHH	16.12	21406692
535	Phosphorylation	TLREAKKSSSISSFK HHHHHHHHCCCHHCC	28.72	29978859
536	Phosphorylation	LREAKKSSSISSFKD HHHHHHHCCCHHCCC	40.34	29978859
537	Phosphorylation	REAKKSSSISSFKDP HHHHHHCCCHHCCCC	33.31	29978859
539	Phosphorylation	AKKSSSISSFKDPKI HHHHCCCHHCCCCCC	31.50	20068231
540	Phosphorylation	KKSSSISSFKDPKIS HHHCCCHHCCCCCCC	34.35	29978859
542	Acetylation	SSSISSFKDPKISTS HCCCHHCCCCCCCCC	75.07	19608861
542	Ubiquitination	SSSISSFKDPKISTS HCCCHHCCCCCCCCC	75.07	21906983
545	Ubiquitination	ISSFKDPKISTSLPV CHHCCCCCCCCCCCH	60.46	-
547	Phosphorylation	SFKDPKISTSLPVLD HCCCCCCCCCCCHHH	20.33	20068231
548	O-linked_Glycosylation	FKDPKISTSLPVLDL CCCCCCCCCCCHHHH	37.44	32870666
548	Phosphorylation	FKDPKISTSLPVLDL CCCCCCCCCCCHHHH	37.44	20068231
549	O-linked_Glycosylation	KDPKISTSLPVLDLI CCCCCCCCCCHHHHH	24.72	32870666
549	Phosphorylation	KDPKISTSLPVLDLI CCCCCCCCCCHHHHH	24.72	20068231
563	Phosphorylation	IDAIQPGSINYDLLK HHHHCCCCCCHHHHC	17.84	20068231
566	Phosphorylation	IQPGSINYDLLKTEN HCCCCCCHHHHCCCC	13.29	20068231
579	Acetylation	ENLNDDEKLNNAKYA CCCCCHHHHHHHHHH	64.61	19608861
579	Ubiquitination	ENLNDDEKLNNAKYA CCCCCHHHHHHHHHH	64.61	19608861
584	Acetylation	DEKLNNAKYAISMAR HHHHHHHHHHHHHHH	37.02	25953088
584	Ubiquitination	DEKLNNAKYAISMAR HHHHHHHHHHHHHHH	37.02	21890473
589	Sulfoxidation	NAKYAISMARKIGAR HHHHHHHHHHHHCCE	3.23	21406390
598	Nitration	RKIGARVYALPEDLV HHHCCEEEECCHHHH	9.25	-
598	Phosphorylation	RKIGARVYALPEDLV HHHCCEEEECCHHHH	9.25	25147952
610	Ubiquitination	DLVEVNPKMVMTVFA HHHCCCHHHHHHHHH	38.63	-
614	Phosphorylation	VNPKMVMTVFACLMG CCHHHHHHHHHHHHC	10.89	22817900

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
5	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
5	S	Phosphorylation	Kinase	PKCA	P17252	PSP
5	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
5	S	Phosphorylation	Kinase	RPS6KA1	Q15418	GPS
5	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
5	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
5	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
7	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
7	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RD23B_HUMAN	RAD23B	physical	22939629
CNDP2_HUMAN	CNDP2	physical	26344197
PLSI_HUMAN	PLS1	physical	28514442
PLST_HUMAN	PLS3	physical	28514442
RNF41_HUMAN	RNF41	physical	28514442
TTL_HUMAN	TTL	physical	28514442

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 PLSL_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-76; LYS-88; LYS-294;LYS-297; LYS-361; LYS-472; LYS-542 AND LYS-579, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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 SER-5; SER-7; TYR-28 ANDSER-30, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Costimulation induced phosphorylation of L-plastin facilitatessurface transport of the T cell activation molecules CD69 and CD25."; Wabnitz G.H., Koecher T., Lohneis P., Stober C., Konstandin M.H.,Funk B., Sester U., Wilm M., Klemke M., Samstag Y.; Eur. J. Immunol. 37:649-662(2007). Cited for: SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF SER-5, PHOSPHORYLATIONAT SER-5, AND MASS SPECTROMETRY.	17294403 [Abstract]
"Phosphorylation on Ser5 increases the F-actin-binding activity of L-plastin and promotes its targeting to sites of actin assembly incells."; Janji B., Giganti A., De Corte V., Catillon M., Bruyneel E., Lentz D.,Plastino J., Gettemans J., Friederich E.; J. Cell Sci. 119:1947-1960(2006). Cited for: FUNCTION, ACTIN-BINDING, INTERACTION WITH ACTIN FIBERS, SUBCELLULARLOCATION, MUTAGENESIS OF SER-5, AND PHOSPHORYLATION AT SER-5.	16636079 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-28 AND TYR-276, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, AND MASSSPECTROMETRY.	15592455 [Abstract]