dbPTM

PLSL_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PLSL_MOUSE
UniProt AC	Q61233
Protein Name	Plastin-2
Gene Name	Lcp1
Organism	Mus musculus (Mouse).
Sequence Length	627
Subcellular Localization	Cytoplasm, cytoskeleton . Cell projection. Cell junction. Cell projection, ruffle membrane Peripheral membrane protein Cytoplasmic side . Relocalizes to the immunological synapse between peripheral blood T-lymphocytes and antibody-presenting cell
Protein Description	Actin-binding protein. Plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. Modulates the cell surface expression of IL2RA/CD25 and CD69..
Protein Sequence	MARGSVSDEEMMELREAFAKVDTDGNGYISCNELNDLFKAACLPLPGYRVREITENLMATGDLDQDGKISFDEFIKVFHGLKSTEVAKTFRKAINKKEGICAIGGTSEQSSVGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDERTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIELSRNEALIALLREGESLEDLMKLSPEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKGDEEGIPAVVIDMSGLREKDDIQRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYPALHKPENQDIDWGALEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGGNMKKLENCNYAVDLGKNQAKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLNILEDIGGGQKVNDDIIVNWVNTTLKEAQKSSSIASFKDPKISTSLPVLDLIDAIQPGSINYDLLKTENLDDEEKLNNAKYAISMARKIGARVYALPEDLVEVNPKMVMTVFACLMGKGMKRV

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	25521595
7	Phosphorylation	-MARGSVSDEEMMEL -CCCCCCCHHHHHHH	40.79	25521595
12	Oxidation	SVSDEEMMELREAFA CCCHHHHHHHHHHHH	5.06	17242355
23	Phosphorylation	EAFAKVDTDGNGYIS HHHHCCCCCCCCEEE	49.12	25367039
28	Phosphorylation	VDTDGNGYISCNELN CCCCCCCEEEHHHHH	8.15	22345495
30	Phosphorylation	TDGNGYISCNELNDL CCCCCEEEHHHHHHH	11.47	26745281
31	S-nitrosocysteine	DGNGYISCNELNDLF CCCCEEEHHHHHHHH	3.13	-
31	S-nitrosylation	DGNGYISCNELNDLF CCCCEEEHHHHHHHH	3.13	24926564
31	Glutathionylation	DGNGYISCNELNDLF CCCCEEEHHHHHHHH	3.13	24333276
39	Ubiquitination	NELNDLFKAACLPLP HHHHHHHHHHHCCCC	42.23	-
42	Glutathionylation	NDLFKAACLPLPGYR HHHHHHHHCCCCCCC	4.86	24333276
48	Phosphorylation	ACLPLPGYRVREITE HHCCCCCCCHHHHHH	12.19	25367039
76	Acetylation	ISFDEFIKVFHGLKS CCHHHHHHHHHCCCC	44.14	-
76	Ubiquitination	ISFDEFIKVFHGLKS CCHHHHHHHHHCCCC	44.14	-
82	Malonylation	IKVFHGLKSTEVAKT HHHHHCCCCHHHHHH	60.98	26320211
83	Phosphorylation	KVFHGLKSTEVAKTF HHHHCCCCHHHHHHH	34.54	29176673
84	Phosphorylation	VFHGLKSTEVAKTFR HHHCCCCHHHHHHHH	32.65	29176673
88	Acetylation	LKSTEVAKTFRKAIN CCCHHHHHHHHHHHH	54.06	-
88	Malonylation	LKSTEVAKTFRKAIN CCCHHHHHHHHHHHH	54.06	26320211
89	Phosphorylation	KSTEVAKTFRKAINK CCHHHHHHHHHHHHH	20.95	18266315
97	Malonylation	FRKAINKKEGICAIG HHHHHHHCCCEEEEC	57.60	26320211
101	Glutathionylation	INKKEGICAIGGTSE HHHCCCEEEECCCCC	3.12	24333276
106	Phosphorylation	GICAIGGTSEQSSVG CEEEECCCCCCCCCC	24.71	30635358
107	Phosphorylation	ICAIGGTSEQSSVGT EEEECCCCCCCCCCC	36.59	30635358
110	Phosphorylation	IGGTSEQSSVGTQHS ECCCCCCCCCCCCCC	23.96	30635358
111	Phosphorylation	GGTSEQSSVGTQHSY CCCCCCCCCCCCCCC	25.02	30635358
114	Phosphorylation	SEQSSVGTQHSYSEE CCCCCCCCCCCCCHH	22.43	30635358
117	Phosphorylation	SSVGTQHSYSEEEKY CCCCCCCCCCHHHHH	22.12	30635358
118	Phosphorylation	SVGTQHSYSEEEKYA CCCCCCCCCHHHHHH	20.27	30635358
119	Phosphorylation	VGTQHSYSEEEKYAF CCCCCCCCHHHHHHH	41.36	30635358
124	Phosphorylation	SYSEEEKYAFVNWIN CCCHHHHHHHHHHHH	14.46	27180971
140	S-nitrosylation	ALENDPDCRHVIPMN HHHCCCCCCCCCCCC	3.84	24926564
164	Glutathionylation	VGDGIVLCKMINLSV HCCCHHEEEECCCCC	1.62	24333276
257	Phosphorylation	ALLREGESLEDLMKL HHHHCCCCHHHHHHC	48.17	25521595
262	Oxidation	GESLEDLMKLSPEEL CCCHHHHHHCCHHHH	6.76	17242355
263	Ubiquitination	ESLEDLMKLSPEELL CCHHHHHHCCHHHHH	53.78	-
265	Phosphorylation	LEDLMKLSPEELLLR HHHHHHCCHHHHHHH	25.42	27180971
276	Phosphorylation	LLLRWANYHLENAGC HHHHHHHHHHHHCCC	10.47	28725479
283	Glutathionylation	YHLENAGCTKITNFS HHHHHCCCCEEEECC	3.04	24333276
290	Phosphorylation	CTKITNFSTDIKDSK CCEEEECCCCCCCCH	27.52	25266776
291	Phosphorylation	TKITNFSTDIKDSKA CEEEECCCCCCCCHH	37.29	29472430
294	Acetylation	TNFSTDIKDSKAYYH EECCCCCCCCHHHHH	59.78	23954790
297	Acetylation	STDIKDSKAYYHLLE CCCCCCCHHHHHHHH	51.01	-
297	Ubiquitination	STDIKDSKAYYHLLE CCCCCCCHHHHHHHH	51.01	-
299	Phosphorylation	DIKDSKAYYHLLEQV CCCCCHHHHHHHHHH	8.64	28725479
300	Phosphorylation	IKDSKAYYHLLEQVA CCCCHHHHHHHHHHC	7.28	25159016
323	Phosphorylation	PAVVIDMSGLREKDD CEEEEECCCCCCHHH	30.81	19854140
336	S-nitrosocysteine	DDIQRAECMLQQAER HHHHHHHHHHHHHHH	3.00	-
336	S-nitrosylation	DDIQRAECMLQQAER HHHHHHHHHHHHHHH	3.00	24926564
336	Glutathionylation	DDIQRAECMLQQAER HHHHHHHHHHHHHHH	3.00	24333276
346	Glutathionylation	QQAERLGCRQFVTAT HHHHHHCCCCEEEHH	3.51	24333276
353	Phosphorylation	CRQFVTATDVVRGNP CCCEEEHHHHHCCCC	21.69	-
361	Acetylation	DVVRGNPKLNLAFIA HHHCCCCCCCHHHHH	54.74	-
406	Phosphorylation	TFRNWMNSLGVNPRV HHHHHHHHCCCCCCH	15.47	27180971
417	Phosphorylation	NPRVNHLYSDLSDAL CCCHHHHHCCHHHHH	7.81	22345495
418	Phosphorylation	PRVNHLYSDLSDALV CCHHHHHCCHHHHHH	38.13	22345495
421	Phosphorylation	NHLYSDLSDALVIFQ HHHHCCHHHHHHHHH	26.31	22345495
444	Malonylation	VDWNRVNKPPYPKLG CCHHHCCCCCCCCCC	44.50	26320211
460	Glutathionylation	NMKKLENCNYAVDLG CCHHHCCCCEEEECC	2.77	24333276
460	S-palmitoylation	NMKKLENCNYAVDLG CCHHHCCCCEEEECC	2.77	26165157
468	Malonylation	NYAVDLGKNQAKFSL CEEEECCCCCCEEEE	53.86	26320211
472	Acetylation	DLGKNQAKFSLVGIA ECCCCCCEEEEEEEE	26.23	-
474	Phosphorylation	GKNQAKFSLVGIAGQ CCCCCEEEEEEEECC	22.80	27180971
530	Ubiquitination	NWVNTTLKEAQKSSS HCHHCHHHHHHHHCC	49.24	-
535	Phosphorylation	TLKEAQKSSSIASFK HHHHHHHHCCCCCCC	19.76	20531401
536	Phosphorylation	LKEAQKSSSIASFKD HHHHHHHCCCCCCCC	32.57	24719451
537	Phosphorylation	KEAQKSSSIASFKDP HHHHHHCCCCCCCCC	29.30	22942356
540	Phosphorylation	QKSSSIASFKDPKIS HHHCCCCCCCCCCCC	31.03	20531401
542	Succinylation	SSSIASFKDPKISTS HCCCCCCCCCCCCCC	71.30	23954790
542	Malonylation	SSSIASFKDPKISTS HCCCCCCCCCCCCCC	71.30	26320211
542	Acetylation	SSSIASFKDPKISTS HCCCCCCCCCCCCCC	71.30	-
579	Acetylation	ENLDDEEKLNNAKYA CCCCCHHHHHHHHHH	55.24	23954790
584	Ubiquitination	EEKLNNAKYAISMAR HHHHHHHHHHHHHHH	37.02	-
589	Sulfoxidation	NAKYAISMARKIGAR HHHHHHHHHHHHCCE	3.23	21406390
598	Phosphorylation	RKIGARVYALPEDLV HHHCCEEEECCHHHH	9.25	28833060
614	Phosphorylation	VNPKMVMTVFACLMG CCHHHHHHHHHHHHC	10.89	25159016
618	Glutathionylation	MVMTVFACLMGKGMK HHHHHHHHHHCCCCC	1.50	24333276

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
89	T	Phosphorylation	Kinase	STK4	Q13043	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
ATX2_MOUSE	Atxn2	physical	16115810

Drug and Disease Associations

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

Regulatory Network of PLSL_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-5, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line."; Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; Mol. Cell. Proteomics 3:279-286(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASSSPECTROMETRY.	14729942 [Abstract]
"Complete primary structure and phosphorylation site of the 65-kDamacrophage protein phosphorylated by stimulation with bacteriallipopolysaccharide."; Shinomiya H., Hagi A., Fukuzumi M., Mizobuchi M., Hirata H.,Utsumi S.; J. Immunol. 154:3471-3478(1995). Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ANDPHOSPHORYLATION AT SER-5 AND SER-7.	7897227 [Abstract]