Tag | Content |
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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 |
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10 | PNCARCGKIVYPTEK | ubiquitination | [1] | 17 | KIVYPTEKVNCLDKF | ubiquitination | [1] | 23 | EKVNCLDKFWHKACF | ubiquitination | [1, 2] | 42 | CKMTLNMKNYKGYEK | ubiquitination | [1] | 59 | YCNAHYPKQSFTMVA | ubiquitination | [1] | 75 | TPENLRLKQQSELQS | ubiquitination | [1] | 96 | EFEKNKGKGFSVVAD | ubiquitination | [1] | 121 | QDQISNIKYHEEFEK | ubiquitination | [1, 2] |
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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. |
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