UniProt Accession

 LIMA1_HUMAN; Q9UHB6; B2RB09; Q2TAN7; Q9BVF2; Q9H8J1; Q9HBN5; Q9NX96; Q9NXC3; Q9NXU6; Q9P0H8; Q9UHB5 

Genbank Protein ID

 AF198454; AF198455; AF157325; AL136911; AK000372; AK000335; AK023649; AK000057; AK314447; CH471111; BC001247; BC010664; BC110815; BC136763; AF218025 

Genbank Nucleotide ID

 AAF23755.1; AAF23756.1; AAF67491.1; CAB66845.1; BAA91120.1; BAA91092.1; BAB14625.1; BAA90914.1; BAG37056.1; EAW58135.1; AAH01247.2; AAH10664.1; AAI10816.1; AAI36764.1; AAG17267.1 

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
21	LSLRVTAKELSLVNK	ubiquitination	[1]
40	AIVEIFSKYQKAAEE	ubiquitination	[1]
75	TLTVLKKKWENPGLG	ubiquitination	[1]
186	ENTDASGKIEKYNVP	ubiquitination	[2]
280	KYQAAVSKQSSSTNY	ubiquitination	[2]
292	TNYTNELKASGGEIK	ubiquitination	[2]
462	GFGHRPHKDLWASKN	ubiquitination	[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

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