CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004173
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Plastin-2 
Protein Synonyms/Alias
 L-plastin; LC64P; Lymphocyte cytosolic protein 1; LCP-1 
Gene Name
 LCP1 
Gene Synonyms/Alias
 PLS2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
76ISFDEFIKIFHGLKSacetylation[1]
76ISFDEFIKIFHGLKSubiquitination[2, 3, 4]
82IKIFHGLKSTDVAKTacetylation[4]
82IKIFHGLKSTDVAKTubiquitination[2, 3, 4, 5]
88LKSTDVAKTFRKAINacetylation[1, 4]
88LKSTDVAKTFRKAINubiquitination[2, 3, 4]
97FRKAINKKEGICAIGubiquitination[2]
132AFVNWINKALENDPDubiquitination[2, 3]
285LENAGCNKIGNFSTDubiquitination[2]
294GNFSTDIKDSKAYYHacetylation[1, 4]
297STDIKDSKAYYHLLEacetylation[1]
297STDIKDSKAYYHLLEubiquitination[2]
361DVVRGNPKLNLAFIAacetylation[1]
361DVVRGNPKLNLAFIAubiquitination[3, 4]
379NRYPALHKPENQDIDubiquitination[3, 4]
434FQLYEKIKVPVDWNRubiquitination[3, 4]
444VDWNRVNKPPYPKLGubiquitination[3]
456KLGGNMKKLENCNYAubiquitination[3, 5]
468NYAVELGKNQAKFSLacetylation[1]
468NYAVELGKNQAKFSLubiquitination[3, 4]
472ELGKNQAKFSLVGIGacetylation[1]
472ELGKNQAKFSLVGIGubiquitination[3]
542SSSISSFKDPKISTSacetylation[1]
542SSSISSFKDPKISTSubiquitination[3, 5, 6]
545ISSFKDPKISTSLPVubiquitination[3]
579ENLNDDEKLNNAKYAacetylation[1]
579ENLNDDEKLNNAKYAubiquitination[3]
584DEKLNNAKYAISMARubiquitination[2, 3]
610DLVEVNPKMVMTVFAubiquitination[3, 5]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional 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. 
Sequence Annotation
 DOMAIN 9 44 EF-hand 1.
 DOMAIN 49 84 EF-hand 2.
 DOMAIN 106 379 Actin-binding 1.
 DOMAIN 120 236 CH 1.
 DOMAIN 264 375 CH 2.
 DOMAIN 380 624 Actin-binding 2.
 DOMAIN 394 503 CH 3.
 DOMAIN 515 624 CH 4.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 5 5 Phosphoserine.
 MOD_RES 7 7 Phosphoserine.
 MOD_RES 28 28 Phosphotyrosine.
 MOD_RES 30 30 Phosphoserine.
 MOD_RES 76 76 N6-acetyllysine.
 MOD_RES 88 88 N6-acetyllysine.
 MOD_RES 124 124 Phosphotyrosine.
 MOD_RES 257 257 Phosphoserine.
 MOD_RES 294 294 N6-acetyllysine.
 MOD_RES 297 297 N6-acetyllysine.
 MOD_RES 323 323 Phosphoserine.
 MOD_RES 361 361 N6-acetyllysine.
 MOD_RES 472 472 N6-acetyllysine.
 MOD_RES 542 542 N6-acetyllysine.
 MOD_RES 579 579 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Actin-binding; Calcium; Cell junction; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 627 AA 
Protein Sequence
MARGSVSDEE MMELREAFAK VDTDGNGYIS FNELNDLFKA ACLPLPGYRV REITENLMAT 60
GDLDQDGRIS FDEFIKIFHG LKSTDVAKTF RKAINKKEGI CAIGGTSEQS SVGTQHSYSE 120
EEKYAFVNWI NKALENDPDC RHVIPMNPNT NDLFNAVGDG IVLCKMINLS VPDTIDERTI 180
NKKKLTPFTI QENLNLALNS ASAIGCHVVN IGAEDLKEGK PYLVLGLLWQ VIKIGLFADI 240
ELSRNEALIA LLREGESLED LMKLSPEELL LRWANYHLEN AGCNKIGNFS TDIKDSKAYY 300
HLLEQVAPKG DEEGVPAVVI DMSGLREKDD IQRAECMLQQ AERLGCRQFV TATDVVRGNP 360
KLNLAFIANL FNRYPALHKP ENQDIDWGAL EGETREERTF RNWMNSLGVN PRVNHLYSDL 420
SDALVIFQLY EKIKVPVDWN RVNKPPYPKL GGNMKKLENC NYAVELGKNQ AKFSLVGIGG 480
QDLNEGNRTL TLALIWQLMR RYTLNILEEI GGGQKVNDDI IVNWVNETLR EAKKSSSISS 540
FKDPKISTSL PVLDLIDAIQ PGSINYDLLK TENLNDDEKL NNAKYAISMA RKIGARVYAL 600
PEDLVEVNPK MVMTVFACLM GKGMKRV 627 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IDA:HPA.
 GO:0005884; C:actin filament; IEA:Compara.
 GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0001891; C:phagocytic cup; IEA:Compara.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
 GO:0003779; F:actin binding; NAS:UniProtKB.
 GO:0005509; F:calcium ion binding; NAS:UniProtKB.
 GO:0051017; P:actin filament bundle assembly; IEA:Compara.
 GO:0031100; P:organ regeneration; IEA:Compara.
 GO:0033157; P:regulation of intracellular protein transport; IDA:UniProtKB.
 GO:0002286; P:T cell activation involved in immune response; IDA:UniProtKB. 
Interpro
 IPR001589; Actinin_actin-bd_CS.
 IPR001715; CH-domain.
 IPR011992; EF-hand-like_dom.
 IPR018247; EF_Hand_1_Ca_BS.
 IPR002048; EF_hand_dom. 
Pfam
 PF00307; CH
 PF00036; efhand 
SMART
 SM00033; CH
 SM00054; EFh 
PROSITE
 PS00019; ACTININ_1
 PS00020; ACTININ_2
 PS50021; CH
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2 
PRINTS