Reviewed,
UniProtKB/Swiss-Prot Q14847 (LASP1_HUMAN)
Last modified
November 25, 2008.
Version 82.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: LIM and SH3 domain protein 1 Short name=LASP-1 Alternative name(s): MLN 50 | ||||
| Gene names |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 261 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | 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. |
| Subunit structure | Interacts with F-actin By similarity. |
| Subcellular location | Cytoplasm › cell cortexBy similarity. Cytoplasm › cytoskeletonBy similarity. Note= Associated with the F-actin rich cortical cytoskeleton By similarity. |
| Post-translational modification | Phosphorylated By similarity. |
| Sequence similarities | Contains 1 LIM zinc-binding domain. Contains 2 nebulin repeats. Contains 1 SH3 domain. |
Ontologies
Keywords | |
|---|---|
| Biological process | Ion transport Transport |
| Cellular component | Cytoplasm Cytoskeleton |
| Coding sequence diversity | Alternative splicing |
| Domain | LIM domain Repeat SH3 domain |
| Ligand | Actin-binding Metal-binding Zinc |
| PTM | Acetylation Phosphoprotein |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | ion transport Inferred from sequence or structural similarity. Source: UniProtKB |
| Cellular component | cortical actin cytoskeleton Inferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | SH3/SH2 adaptor activity Ref.4 Traceable author statement. Source: ProtInc actin bindingInferred from electronic annotation. Source: UniProtKB-KW ion transmembrane transporter activityInferred from sequence or structural similarity. Source: UniProtKB zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q14847-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q14847-2) The sequence of this isoform differs from the canonical sequence as follows: 201-261: GGGGKRYRAV...MLPANYVEAI → ICLQHIPRHR...LTYPHIPGLG | ||||||
| Notes: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 261 | 261 | LIM and SH3 domain protein 1 | PRO_0000075761 | |||||
Regions | |||||||||
| Domain | 5 – 56 | 52 | LIM zinc-binding | ||||||
| Repeat | 61 – 95 | 35 | Nebulin 1 | ||||||
| Repeat | 97 – 131 | 35 | Nebulin 2 | ||||||
| Domain | 202 – 261 | 60 | SH3 | ||||||
| Compositional bias | 201 – 204 | 4 | Poly-Gly | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine | ||||||
| Modified residue | 68 | 1 | Phosphothreonine | ||||||
| Modified residue | 104 | 1 | Phosphothreonine | ||||||
| Modified residue | 146 | 1 | Phosphoserine | ||||||
| Modified residue | 151 | 1 | Phosphoserine | ||||||
| Modified residue | 171 | 1 | Phosphotyrosine | ||||||
Natural variations | |||||||||
| Alternative sequence | 201 – 261 | 61 | GGGGK…YVEAI → ICLQHIPRHRIRPGRDPSIL QCLCFLKPATACDSYPSSSF FCQLKPSSATSAGSLLWQAS PLIDFLVFSLDGTGMGLSGG GRGPWGRAGMGDLLACGPHL PLCSLPSHPPAQLLTYPHIP GLG in isoform 2. | VSP_016554 | |||||
Experimental info | |||||||||
| Sequence conflict | 79 | 1 | E → R in AAH12460. Ref.2 | ||||||
| Sequence conflict | 210 | 1 | V → A in AAH12460. Ref.2 | ||||||
| Sequence conflict | 220 | 1 | E → A in AAH12460. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification of four novel human genes amplified and overexpressed in breast carcinoma and localized to the q11-q21.3 region of chromosome 17." Tomasetto C.L., Regnier C.H., Moog-Lutz C., Mattei M.-G., Chenard M.-P., Lidereau R., Basset P., Rio M.-C. Genomics 28:367-376(1995) [PubMed: 7490069] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Mammary carcinoma. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Liver and Skin. |
| [3] | "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-7, ACETYLATION AT MET-1. Tissue: Platelet. |
| [4] | "Lasp-1 (MLN 50) defines a new LIM protein subfamily characterized by the association of LIM and SH3 domains." Tomasetto C., Moog-Lutz C., Regnier C.H., Schreiber V., Basset P., Rio M.-C. FEBS Lett. 373:245-249(1995) [PubMed: 7589475] [Abstract] Cited for: DOMAINS. |
| [5] | "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-171, MASS SPECTROMETRY. Tissue: T-cell. |
| [6] | "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68; THR-104 AND SER-151, MASS SPECTROMETRY. Tissue: Epithelium. |
| [7] | "Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, MASS SPECTROMETRY. Tissue: Platelet. |
| [8] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68; THR-104 AND SER-146, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| X82456 mRNA. Translation: CAA57833.1. BC007560 mRNA. Translation: AAH07560.1. BC012460 mRNA. Translation: AAH12460.1. | |
| PIR | S68234. |
| RefSeq | NP_006139.1. |
| UniGene | Hs.548018 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1ZFO based on UniProtKB P80171. |
| SMR | Q14847. Positions 203-261. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q14847. |
PTM databases | |
| PhosphoSite | Q14847. |
2-D gel databases | |
| SWISS-2DPAGE | Q14847. |
| OGP | Q14847. |
Genome annotation databases | |
| Ensembl | ENSG00000002834. Homo sapiens. [Contig view] |
| GeneID | 3927. |
| KEGG | hsa:3927. |
Organism-specific databases | |
| H-InvDB | HIX0013769. |
| HGNC | HGNC:6513. LASP1. |
| HPA | HPA012072. |
| MIM | 602920. gene. |
| PharmGKB | PA38436. |
| GenAtlas | Search... |
| GeneCards | Search... |
Phylogenomic databases | |
| HOVERGEN | Q14847. |
Gene expression databases | |
| ArrayExpress | Q14847. |
| CleanEx | HS_LASP1. |
| GermOnline | ENSG00000002834. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR013998. Nebulin. IPR000900. Nebulin_35r-motif. IPR001452. SH3. IPR001781. Znf_LIM. [Graphical view] |
| Gene3D | G3DSA:2.10.110.10. Znf_LIM. 1 hit. |
| PANTHER | PTHR11039. Nebulin. 1 hit. |
| Pfam | PF00412. LIM. 1 hit. PF00880. Nebulin. 2 hits. PF00018. SH3_1. 1 hit. [Graphical view] |
| PRINTS | PR00452. SH3DOMAIN. |
| ProDom | PD000094. LIM. 1 hit. PD000066. SH3. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00132. LIM. 1 hit. SM00227. NEBU. 2 hits. SM00326. SH3. 1 hit. [Graphical view] |
| PROSITE | PS00478. LIM_DOMAIN_1. 1 hit. PS50023. LIM_DOMAIN_2. 1 hit. PS51216. NEBULIN. 2 hits. PS50002. SH3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| LinkHub | Q14847. |
| NextBio | 15423. |
| SOURCE | Search... |
Entry information
| Entry name | LASP1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q14847 Secondary accession number(s): Q96ED2, Q96IG0 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 17 Human chromosome 17: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| UniProtKB secondary accession numbers Index of UniProtKB secondary accession numbers |
| SIMILARITY comments Index of protein domains and families |

Clusters with


