CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012402
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 LIM and SH3 domain protein 1 
Protein Synonyms/Alias
 LASP-1; Metastatic lymph node gene 50 protein; MLN 50 
Gene Name
 LASP1 
Gene Synonyms/Alias
 MLN50 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
10PNCARCGKIVYPTEKubiquitination[1]
17KIVYPTEKVNCLDKFubiquitination[1]
23EKVNCLDKFWHKACFubiquitination[1, 2]
42CKMTLNMKNYKGYEKubiquitination[1]
59YCNAHYPKQSFTMVAubiquitination[1]
75TPENLRLKQQSELQSubiquitination[1]
96EFEKNKGKGFSVVADubiquitination[1]
121QDQISNIKYHEEFEKubiquitination[1, 2]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] 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
Functional Description
 Plays an important role in the regulation of dynamic actin-based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation may also serve to regulate actin-associated ion transport activities, not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell types (By similarity). 
Sequence Annotation
 DOMAIN 5 56 LIM zinc-binding.
 REPEAT 61 95 Nebulin 1.
 REPEAT 97 131 Nebulin 2.
 DOMAIN 202 261 SH3.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 42 42 N6-acetyllysine.
 MOD_RES 68 68 Phosphothreonine.
 MOD_RES 104 104 Phosphothreonine.
 MOD_RES 118 118 Phosphoserine.
 MOD_RES 146 146 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Actin-binding; Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Ion transport; LIM domain; Metal-binding; Phosphoprotein; Reference proteome; Repeat; SH3 domain; Transport; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 261 AA 
Protein Sequence
MNPNCARCGK IVYPTEKVNC LDKFWHKACF HCETCKMTLN MKNYKGYEKK PYCNAHYPKQ 60
SFTMVADTPE NLRLKQQSEL QSQVRYKEEF EKNKGKGFSV VADTPELQRI KKTQDQISNI 120
KYHEEFEKSR MGPSGGEGME PERRDSQDGS SYRRPLEQQQ PHHIPTSAPV YQQPQQQPVA 180
QSYGGYKEPA APVSIQRSAP ICLQHIPRHR IRPGRDPSIL QCLCFLKPAT ACDSYPSSSF 240
FCQLKPSSAT SAGSLLWQAS PLIDFLVFSL DGTGMGLSGG GRGPWGRAGM GDLLACGPHL 300
PLCSLPSHPP AQLLTYPHIP GLG 323 
Gene Ontology
 GO:0030864; C:cortical actin cytoskeleton; ISS:UniProtKB.
 GO:0005925; C:focal adhesion; IEA:Compara.
 GO:0015075; F:ion transmembrane transporter activity; ISS:UniProtKB.
 GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR000900; Nebulin_35r-motif.
 IPR001452; SH3_domain.
 IPR001781; Znf_LIM. 
Pfam
 PF00412; LIM
 PF00880; Nebulin
 PF00018; SH3_1 
SMART
 SM00132; LIM
 SM00227; NEBU
 SM00326; SH3 
PROSITE
 PS00478; LIM_DOMAIN_1
 PS50023; LIM_DOMAIN_2
 PS51216; NEBULIN
 PS50002; SH3 
PRINTS
 PR00452; SH3DOMAIN.