CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004174
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Plastin-3 
Protein Synonyms/Alias
 T-plastin 
Gene Name
 PLS3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
52NMPLPGYKVREIIQKubiquitination[1, 2]
59KVREIIQKLMLDGDRubiquitination[1]
91VKSSDIAKTFRKAINubiquitination[1, 2]
100FRKAINRKEGICALGubiquitination[1]
168GDGIVLCKMINLSVPubiquitination[1, 3, 4]
266ETLEELMKLSPEELLubiquitination[2, 4]
297NNFSADIKDSKAYFHubiquitination[2]
300SADIKDSKAYFHLLNubiquitination[1, 2]
382NKYPALTKPENQDIDubiquitination[1, 2]
437LQLYERIKVPVDWSKubiquitination[1]
518EDLGDGQKANDDIIVubiquitination[2]
545STSIQSFKDKTISSSubiquitination[2]
587DDKHNNAKYAVSMARubiquitination[2]
611PEDLVEVKPKMVMTVubiquitination[1, 2, 4]
Reference
 [1] 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]
 [2] 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]
 [3] Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry.
 Denis NJ, Vasilescu J, Lambert JP, Smith JC, Figeys D.
 Proteomics. 2007 Mar;7(6):868-74. [PMID: 17370265]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
Functional Description
 Actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. 
Sequence Annotation
 DOMAIN 12 47 EF-hand 1.
 DOMAIN 52 87 EF-hand 2.
 DOMAIN 109 382 Actin-binding 1.
 DOMAIN 123 239 CH 1.
 DOMAIN 267 378 CH 2.
 DOMAIN 383 627 Actin-binding 2.
 DOMAIN 397 506 CH 3.
 DOMAIN 518 627 CH 4.
 MOD_RES 293 293 Phosphoserine.
 MOD_RES 326 326 Phosphoserine.
 MOD_RES 391 391 Phosphothreonine.
 CROSSLNK 168 168 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Actin-binding; Calcium; Complete proteome; Cytoplasm; Direct protein sequencing; Isopeptide bond; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 630 AA 
Protein Sequence
MDEMATTQIS KDELDELKEA FAKVDLNSNG FICDYELHEL FKEANMPLPG YKVREIIQKL 60
MLDGDRNKDG KISFDEFVYI FQEVKSSDIA KTFRKAINRK EGICALGGTS ELSSEGTQHS 120
YSEEEKYAFV NWINKALEND PDCRHVIPMN PNTDDLFKAV GDGIVLCKMI NLSVPDTIDE 180
RAINKKKLTP FIIQENLNLA LNSASAIGCH VVNIGAEDLR AGKPHLVLGL LWQIIKIGLF 240
ADIELSRNEA LAALLRDGET LEELMKLSPE ELLLRWANFH LENSGWQKIN NFSADIKDSK 300
AYFHLLNQIA PKGQKEGEPR IDINMSGFNE TDDLKRAESM LQQADKLGCR QFVTPADVVS 360
GNPKLNLAFV ANLFNKYPAL TKPENQDIDW TLLEGETREE RTFRNWMNSL GVNPHVNHLY 420
ADLQDALVIL QLYERIKVPV DWSKVNKPPY PKLGANMKKL ENCNYAVELG KHPAKFSLVG 480
IGGQDLNDGN QTLTLALVWQ LMRRYTLNVL EDLGDGQKAN DDIIVNWVNR TLSEAGKSTS 540
IQSFKDKTIS SSLAVVDLID AIQPGCINYD LVKSGNLTED DKHNNAKYAV SMARRIGARV 600
YALPEDLVEV KPKMVMTVFA CLMGRGMKRV 630 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005509; F:calcium ion binding; IEA:InterPro. 
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
 PF13499; EF_hand_5 
SMART
 SM00033; CH
 SM00054; EFh 
PROSITE
 PS00019; ACTININ_1
 PS00020; ACTININ_2
 PS50021; CH
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2 
PRINTS