Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Plastin-2  

UniProtKB / Swiss-Prot ID :  PLSL_HUMAN

Gene Name (Synonyms) : 
LCP1, PLS2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cytoskeleton. Cell junction. Cell projection. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). Note=Relocalizes to the immunological synapse between peripheral blood T-lymphocytes and antibody-pr 

Protein Function :  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 MARGSVSDEEMMELREAFAKVDTDGNGYISFNELNDLFKAACLPLPGYRVREITENLMATGDLDQDGRIS...
Predicted Secondary Structure CCCCCCCHHHHHHHHHHHHHHCCCCCCEECHHHHHHHHHHHCCCCCHHHHHHHHHHHHHHHCCCCCCEEC...
Protein Variant
LocationDescription
24D -> E. VAR_001371
533K -> E (in dbSNP:rs4941543). VAR_024398
544P -> A (in dbSNP:rs17067725). VAR_030826
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MARGSV
---CCCCCC
25.25UniProtKB
Link-
5PhosphoserineMARGSVSDE
CCCCCCCHH
16.94Phosphositeplus
Link-
5Phosphoserine (PKA_group)MARGSVSDE
CCCCCCCHH
16.94PhosphoELM
Link-
5Phosphoserine (PRKACA)MARGSVSDE
CCCCCCCHH
16.94HPRD
Link-
5Phosphoserine.MARGSVSDE
CCCCCCCHH
16.94UniProtKB
Link-
7PhosphoserineRGSVSDEEM
CCCCCHHHH
40.79Phosphositeplus
Link-
7Phosphoserine (PKA_group)RGSVSDEEM
CCCCCHHHH
40.79PhosphoELM
Link-
7Phosphoserine.RGSVSDEEM
CCCCCHHHH
40.79UniProtKB
Link-
28PhosphotyrosineDGNGYISFN
CCCCEECHH
9.44HPRD
Link-
28PhosphotyrosineDGNGYISFN
CCCCEECHH
9.44PhosphoELM
Link-
28PhosphotyrosineDGNGYISFN
CCCCEECHH
9.44Phosphositeplus
Link-
28Phosphotyrosine.DGNGYISFN
CCCCEECHH
9.44UniProtKB
Link-
30PhosphoserineNGYISFNEL
CCEECHHHH
17.34Phosphositeplus
Link-
30Phosphoserine.NGYISFNEL
CCEECHHHH
17.34UniProtKB
Link-
76Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DEFIKIFHG
HHHHHHHHH
44.64Phosphositeplus
Link-
76N6-acetyllysineDEFIKIFHG
HHHHHHHHH
44.64HPRD
Link-
76N6-acetyllysineDEFIKIFHG
HHHHHHHHH
44.64Phosphositeplus
Link-
76N6-acetyllysine.DEFIKIFHG
HHHHHHHHH
44.64UniProtKB
Link-
82Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FHGLKSTDV
HHHHCCCCH
56.77Phosphositeplus
Link-
88Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TDVAKTFRK
CCHHHHHHH
48.31Phosphositeplus
Link-
88N6-acetyllysineTDVAKTFRK
CCHHHHHHH
48.31HPRD
Link-
88N6-acetyllysineTDVAKTFRK
CCHHHHHHH
48.31Phosphositeplus
Link-
88N6-acetyllysine.TDVAKTFRK
CCHHHHHHH
48.31UniProtKB
Link-
97Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AINKKEGIC
HHCCCCCCH
57.60Phosphositeplus
Link-
118PhosphotyrosineTQHSYSEEE
HHHHHHHHH
20.27Phosphositeplus
Link-
124PhosphotyrosineEEEKYAFVN
HHHHHHHHH
14.46HPRD
Link-
124PhosphotyrosineEEEKYAFVN
HHHHHHHHH
14.46Phosphositeplus
Link-
124Phosphotyrosine.EEEKYAFVN
HHHHHHHHH
14.46UniProtKB
Link-
165Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IVLCKMINL
HHHHHHHHH
38.36Phosphositeplus
Link-
243PhosphoserineDIELSRNEA
CCEECCCCC
21.92HPRD
Link-
257PhosphoserineREGESLEDL
CCCCCHHHH
48.17HPRD
Link-
257PhosphoserineREGESLEDL
CCCCCHHHH
48.17Phosphositeplus
Link-
276PhosphotyrosineRWANYHLEN
HHHHHHHCC
10.47HPRD
Link-
276PhosphotyrosineRWANYHLEN
HHHHHHHCC
10.47PhosphoELM
Link-
276PhosphotyrosineRWANYHLEN
HHHHHHHCC
10.47Phosphositeplus
Link-
276Phosphotyrosine.RWANYHLEN
HHHHHHHCC
10.47UniProtKB
Link-
285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AGCNKIGNF
CCCCCEEEC
56.94Phosphositeplus
Link-
291PhosphothreonineGNFSTDIKD
EECCCHHHH
37.29Phosphositeplus
Link-
294N6-acetyllysineSTDIKDSKA
CCHHHHHHH
59.78HPRD
Link-
294N6-acetyllysineSTDIKDSKA
CCHHHHHHH
59.78Phosphositeplus
Link-
294N6-acetyllysine.STDIKDSKA
CCHHHHHHH
59.78UniProtKB
Link-
297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IKDSKAYYH
HHHHHHHHH
51.01Phosphositeplus
Link-
297N6-acetyllysineIKDSKAYYH
HHHHHHHHH
51.01HPRD
Link-
297N6-acetyllysineIKDSKAYYH
HHHHHHHHH
51.01Phosphositeplus
Link-
297N6-acetyllysine.IKDSKAYYH
HHHHHHHHH
51.01UniProtKB
Link-
323PhosphoserineVIDMSGLRE
CCCCHHCCC
30.81Phosphositeplus
Link-
361N6-acetyllysineRGNPKLNLA
CCCHHHHHH
54.74HPRD
Link-
361N6-acetyllysineRGNPKLNLA
CCCHHHHHH
54.74Phosphositeplus
Link-
361N6-acetyllysine.RGNPKLNLA
CCCHHHHHH
54.74UniProtKB
Link-
374PhosphotyrosineLFNRYPALH
HHHHCCCCC
8.25Phosphositeplus
Link-
430PhosphotyrosineIFQLYEKIK
HHHHHHHHH
12.37Phosphositeplus
Link-
468N6-acetyllysineVELGKNQAK
HHHHHCCCC
59.52HPRD
Link-
472N6-acetyllysineKNQAKFSLV
HCCCCEEEC
26.23HPRD
Link-
472N6-acetyllysineKNQAKFSLV
HCCCCEEEC
26.23Phosphositeplus
Link-
472N6-acetyllysine.KNQAKFSLV
HCCCCEEEC
26.23UniProtKB
Link-
537PhosphoserineKKSSSISSF
CCCCCCCCC
33.31HPRD
Link
542Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ISSFKDPKI
CCCCCCCCC
75.07Phosphositeplus
Link
542N6-acetyllysineISSFKDPKI
CCCCCCCCC
75.07HPRD
Link
542N6-acetyllysineISSFKDPKI
CCCCCCCCC
75.07Phosphositeplus
Link
542N6-acetyllysine.ISSFKDPKI
CCCCCCCCC
75.07UniProtKB
Link
579N6-acetyllysineNDDEKLNNA
CCCHHHHHH
64.61HPRD
Link
579N6-acetyllysineNDDEKLNNA
CCCHHHHHH
64.61Phosphositeplus
Link
579N6-acetyllysine.NDDEKLNNA
CCCHHHHHH
64.61UniProtKB
Link
584Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LNNAKYAIS
HHHHHHHHH
37.02Phosphositeplus
Link
598PhosphotyrosineGARVYALPE
CCCEECCHH
9.25Phosphositeplus
Link
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PLSL_HUMANin vitro
in vivo
HPRD:01082HPRD11279160
GRAN_HUMANENSP00000315757STRING
- top -

Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
- top -
Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
"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.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures