CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012181
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Four and a half LIM domains protein 1 
Protein Synonyms/Alias
 FHL-1; Skeletal muscle LIM-protein 1; SLIM; SLIM-1 
Gene Name
 FHL1 
Gene Synonyms/Alias
 SLIM1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
22QGKKYVQKDGHHCCLacetylation[1]
106PKCKGCFKAIVAGDQubiquitination[2, 3]
118GDQNVEYKGTVWHKDacetylation[4]
118GDQNVEYKGTVWHKDubiquitination[2, 3]
Reference
 [1] 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]
 [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] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
 May have an involvement in muscle development or hypertrophy. 
Sequence Annotation
 DOMAIN 40 92 LIM zinc-binding 1.
 DOMAIN 101 153 LIM zinc-binding 2.
 DOMAIN 162 212 LIM zinc-binding 3.
 ZN_FING 7 31 C4-type (Potential).  
Keyword
 3D-structure; Alternative splicing; Cardiomyopathy; Complete proteome; Cytoplasm; Developmental protein; Differentiation; Direct protein sequencing; Disease mutation; LIM domain; Metal-binding; Nucleus; Reference proteome; Repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 323 AA 
Protein Sequence
MAEKFDCHYC RDPLQGKKYV QKDGHHCCLK CFDKFCANTC VECRKPIGAD SKEVHYKNRF 60
WHDTCFRCAK CLHPLANETF VAKDNKILCN KCTTREDSPK CKGCFKAIVA GDQNVEYKGT 120
VWHKDCFTCS NCKQVIGTGS FFPKGEDFYC VTCHETKFAK HCVKCNKAIT SGGITYQDQP 180
WHADCFVCVT CSKKLAGQRF TAVEDQYYCV DCYKNFVAKK CAGCKNPITG KRTVSRVSHP 240
VSKARKPPVC HGKRLPLTLF PSANLRGRHP GGERTCPSWV VVLYRKNRSL AAPRGPGLVK 300
APVWWPMKDN PGTTTASTAK NAP 323 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:BHF-UCL.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0007517; P:muscle organ development; NAS:UniProtKB.
 GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
 GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:UniProtKB.
 GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IDA:UniProtKB.
 GO:0009887; P:organ morphogenesis; NAS:UniProtKB.
 GO:0043268; P:positive regulation of potassium ion transport; IDA:BHF-UCL.
 GO:0003254; P:regulation of membrane depolarization; IDA:BHF-UCL.
 GO:1901016; P:regulation of potassium ion transmembrane transporter activity; IDA:BHF-UCL. 
Interpro
 IPR001781; Znf_LIM. 
Pfam
 PF00412; LIM 
SMART
 SM00132; LIM 
PROSITE
 PS00478; LIM_DOMAIN_1
 PS50023; LIM_DOMAIN_2 
PRINTS