CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022925
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 LIM domain and actin-binding protein 1 
Protein Synonyms/Alias
 Epithelial protein lost in neoplasm 
Gene Name
 LIMA1 
Gene Synonyms/Alias
 EPLIN; SREBP3; PP624 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
21LSLRVTAKELSLVNKubiquitination[1]
40AIVEIFSKYQKAAEEubiquitination[1]
75TLTVLKKKWENPGLGubiquitination[1]
186ENTDASGKIEKYNVPubiquitination[2]
280KYQAAVSKQSSSTNYubiquitination[2]
292TNYTNELKASGGEIKubiquitination[2]
462GFGHRPHKDLWASKNubiquitination[1]
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
Functional Description
 Binds to actin monomers and filaments. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments. 
Sequence Annotation
 DOMAIN 388 448 LIM zinc-binding.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 4 4 Phosphoserine.
 MOD_RES 15 15 Phosphoserine.
 MOD_RES 132 132 Phosphoserine.
 MOD_RES 225 225 Phosphoserine.
 MOD_RES 229 229 Phosphotyrosine.
 MOD_RES 230 230 Phosphoserine (By similarity).
 MOD_RES 263 263 Phosphoserine.
 MOD_RES 343 343 Phosphoserine.
 MOD_RES 350 350 Phosphoserine.
 MOD_RES 362 362 Phosphoserine.
 MOD_RES 365 365 Phosphoserine.
 MOD_RES 369 369 Phosphoserine.
 MOD_RES 374 374 Phosphoserine.
 MOD_RES 490 490 Phosphoserine.
 MOD_RES 541 541 Phosphoserine (By similarity).
 MOD_RES 604 604 Phosphoserine.
 MOD_RES 609 609 Phosphoserine.
 MOD_RES 617 617 Phosphoserine.
 MOD_RES 686 686 Phosphoserine.
 MOD_RES 692 692 Phosphoserine.
 MOD_RES 698 698 Phosphoserine.
 MOD_RES 726 726 Phosphoserine.
 MOD_RES 741 741 Phosphoserine (By similarity).  
Keyword
 3D-structure; Acetylation; Actin-binding; Alternative promoter usage; Alternative splicing; Cell junction; Complete proteome; Cytoplasm; Cytoskeleton; LIM domain; Metal-binding; Phosphoprotein; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 759 AA 
Protein Sequence
MESSPFNRRQ WTSLSLRVTA KELSLVNKNK SSAIVEIFSK YQKAAEETNM EKKRSNTENL 60
SQHFRKGTLT VLKKKWENPG LGAESHTDSL RNSSTEIRHR ADHPPAEVTS HAASGAKADQ 120
EEQIHPRSRL RSPPEALVQG RYPHIKDGED LKDHSTESKK MENCLGESRH EVEKSEISEN 180
TDASGKIEKY NVPLNRLKMM FEKGEPTQTK ILRAQSRSAS GRKISENSYS LDDLEIGPGQ 240
LSSSTFDSEK NESRRNLELP RLSETSIKDR MAKYQAAVSK QSSSTNYTNE LKASGGEIKI 300
HKMEQKENVP PGPEVCITHQ EGEKISANEN SLAVRSTPAE DDSRDSQVKS EVQQPVHPKP 360
LSPDSRASSL SESSPPKAMK KFQAPARETC VECQKTVYPM ERLLANQQVF HISCFRCSYC 420
NNKLSLGTYA SLHGRIYCKP HFNQLFKSKG NYDEGFGHRP HKDLWASKNE NEEILERPAQ 480
LANARETPHS PGVEDAPIAK VGVLAASMEA KASSQQEKED KPAETKKLRI AWPPPTELGS 540
SGSALEEGIK MSKPKWPPED EISKPEVPED VDLDLKKLRR SSSLKERSRP FTVAASFQST 600
SVKSPKTVSP PIRKGWSMSE QSEESVGGRV AERKQVENAK ASKKNGNVGK TTWQNKESKG 660
ETGKRSKEGH SLEMENENLV ENGADSDEDD NSFLKQQSPQ EPKSLNWSSF VDNTFAEEFT 720
TQNQKSQDVE LWEGEVVKEL SVEEQIKRNR YYDEDEDEE 759 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005925; C:focal adhesion; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0001725; C:stress fiber; IDA:UniProtKB.
 GO:0051015; F:actin filament binding; IDA:UniProtKB.
 GO:0003785; F:actin monomer binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0051017; P:actin filament bundle assembly; IDA:UniProtKB.
 GO:0030835; P:negative regulation of actin filament depolymerization; IDA:UniProtKB.
 GO:0031529; P:ruffle organization; IDA:UniProtKB. 
Interpro
 IPR001781; Znf_LIM. 
Pfam
 PF00412; LIM 
SMART
 SM00132; LIM 
PROSITE
 PS00478; LIM_DOMAIN_1
 PS50023; LIM_DOMAIN_2 
PRINTS