LOCUS       NP_057441                759 aa            linear   PRI 29-APR-2025
DEFINITION  LIM domain and actin-binding protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_057441
VERSION     NP_057441.1
DBSOURCE    REFSEQ: accession NM_016357.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Obulkasim,H., Adili,A., Liu,Y. and Duan,S.
  TITLE     Expression and molecular insights of lima1 in cholangiocarcinoma
  JOURNAL   Cell Adh Migr 18 (1), 4-17 (2024)
   PUBMED   39076043
  REMARK    GeneRIF: Expression and molecular insights of lima1 in
            cholangiocarcinoma.
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Hecht,M., Alber,N., Marhoffer,P., Johnsson,N. and Gronemeyer,T.
  TITLE     The concerted action of SEPT9 and EPLIN modulates the adhesion and
            migration of human fibroblasts
  JOURNAL   Life Sci Alliance 7 (7), e202201686 (2024)
   PUBMED   38719752
  REMARK    GeneRIF: The concerted action of SEPT9 and EPLIN modulates the
            adhesion and migration of human fibroblasts.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 759)
  AUTHORS   Liu,Z., Yang,L.Y., Hao,J.J., Zhang,N., Fan,Z.L., Cai,H.Q., Cai,Y.,
            Wei,W.Q., Zhang,Y. and Wang,M.R.
  TITLE     Nuclear-cytoplasmic translocation of SQSTM1/p62 protein enhances
            ESCC cell migration and invasion by stabilizing EPLIN expression
  JOURNAL   Exp Cell Res 435 (1), 113910 (2024)
   PUBMED   38185251
  REMARK    GeneRIF: Nuclear-cytoplasmic translocation of SQSTM1/p62 protein
            enhances ESCC cell migration and invasion by stabilizing EPLIN
            expression.
REFERENCE   4  (residues 1 to 759)
  AUTHORS   Jiang,W., Yang,X., Shi,K., Zhang,Y., Shi,X., Wang,J., Wang,Y.,
            Chenyan,A., Shan,J., Wang,Y., Chang,J., Chen,R., Zhou,T., Zhu,Y.,
            Yu,Y., Li,C. and Li,X.
  TITLE     MAD2 activates IGF1R/PI3K/AKT pathway and promotes
            cholangiocarcinoma progression by interfering USP44/LIMA1 complex
  JOURNAL   Oncogene 42 (45), 3344-3357 (2023)
   PUBMED   37752233
  REMARK    GeneRIF: MAD2 activates IGF1R/PI3K/AKT pathway and promotes
            cholangiocarcinoma progression by interfering USP44/LIMA1 complex.
REFERENCE   5  (residues 1 to 759)
  AUTHORS   Li,D., Neo,S.P., Gunaratne,J. and Sabapathy,K.
  TITLE     EPLIN-beta is a novel substrate of ornithine decarboxylase antizyme
            1 and mediates cellular migration
  JOURNAL   J Cell Sci 136 (12) (2023)
   PUBMED   37325974
  REMARK    GeneRIF: EPLIN-beta is a novel substrate of ornithine decarboxylase
            antizyme 1 and mediates cellular migration.
REFERENCE   6  (residues 1 to 759)
  AUTHORS   Maul,R.S., Song,Y., Amann,K.J., Gerbin,S.C., Pollard,T.D. and
            Chang,D.D.
  TITLE     EPLIN regulates actin dynamics by cross-linking and stabilizing
            filaments
  JOURNAL   J Cell Biol 160 (3), 399-407 (2003)
   PUBMED   12566430
REFERENCE   7  (residues 1 to 759)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   8  (residues 1 to 759)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
REFERENCE   9  (residues 1 to 759)
  AUTHORS   Chen,S., Maul,R.S., Kim,H.R. and Chang,D.D.
  TITLE     Characterization of the human EPLIN (Epithelial Protein Lost in
            Neoplasm) gene reveals distinct promoters for the two EPLIN
            isoforms
  JOURNAL   Gene 248 (1-2), 69-76 (2000)
   PUBMED   10806352
REFERENCE   10 (residues 1 to 759)
  AUTHORS   Maul,R.S. and Chang,D.D.
  TITLE     EPLIN, epithelial protein lost in neoplasm
  JOURNAL   Oncogene 18 (54), 7838-7841 (1999)
   PUBMED   10618726
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP281423.1, BC110815.1 and
            AL136911.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a cytoskeleton-associated protein that
            inhibits actin filament depolymerization and cross-links filaments
            in bundles. It is downregulated in some cancer cell lines.
            Alternatively spliced transcript variants encoding different
            isoforms have been described for this gene, and expression of some
            of the variants maybe independently regulated. [provided by RefSeq,
            Aug 2011].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            acceptor splice site at an internal coding exon compared to variant
            1. This results in an isoform (2, also known as EPLIN-beta) that is
            1 aa shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110815.1, AL136911.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000341247.9/ ENSP00000340184.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..759
                     /product="LIM domain and actin-binding protein 1 isoform
                     2"
                     /note="sterol regulatory element binding protein 3;
                     epithelial protein lost in neoplasm beta"
                     /calculated_mol_wt=85095
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Region          78..131
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Region          146..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Region          164..166
                     /region_name="Required for interaction with NPC1L1.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Region          211..264
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG0; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG0; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Region          323..381
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Region          390..442
                     /region_name="LIM_Eplin_alpha_beta"
                     /note="The Lim domain of Epithelial Protein Lost in
                     Neoplasm (Eplin); cd09485"
                     /db_xref="CDD:188869"
     Site            order(390,393,411,414,417,420,438,441)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188869"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Region          493..513
                     /region_name="Required for interaction with MYO5B.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Region          509..709
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            601
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            604
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            609
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            617
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            686
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            698
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            726
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     Site            741
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG0; propagated from
                     UniProtKB/Swiss-Prot (Q9UHB6.1)"
     CDS             1..759
                     /gene="LIMA1"
                     /gene_synonym="EPLIN; LDLCQ8; SREBP3"
                     /coded_by="NM_016357.5:125..2404"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS8802.1"
                     /db_xref="GeneID:51474"
                     /db_xref="HGNC:HGNC:24636"
                     /db_xref="MIM:608364"
ORIGIN      
        1 messpfnrrq wtslslrvta kelslvnknk ssaiveifsk yqkaaeetnm ekkrsntenl
       61 sqhfrkgtlt vlkkkwenpg lgaeshtdsl rnssteirhr adhppaevts haasgakadq
      121 eeqihprsrl rsppealvqg ryphikdged lkdhsteskk menclgesrh evekseisen
      181 tdasgkieky nvplnrlkmm fekgeptqtk ilraqsrsas grkisensys lddleigpgq
      241 lssstfdsek nesrrnlelp rlsetsikdr makyqaavsk qssstnytne lkasggeiki
      301 hkmeqkenvp pgpevcithq egekisanen slavrstpae ddsrdsqvks evqqpvhpkp
      361 lspdsrassl sessppkamk kfqaparetc vecqktvypm erllanqqvf hiscfrcsyc
      421 nnklslgtya slhgriyckp hfnqlfkskg nydegfghrp hkdlwaskne neeilerpaq
      481 lanaretphs pgvedapiak vgvlaasmea kassqqeked kpaetkklri awppptelgs
      541 sgsaleegik mskpkwpped eiskpevped vdldlkklrr ssslkersrp ftvaasfqst
      601 svkspktvsp pirkgwsmse qseesvggrv aerkqvenak askkngnvgk ttwqnkeskg
      661 etgkrskegh slemenenlv engadsdedd nsflkqqspq epkslnwssf vdntfaeeft
      721 tqnqksqdve lwegevvkel sveeqikrnr yydededee
//
