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Q14847 (LASP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
LIM and SH3 domain protein 1

Short name=LASP-1
Alternative name(s):
Metastatic lymph node gene 50 protein
Short name=MLN 50
Gene names
Name:LASP1
Synonyms:MLN50
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Interacts with ANKRD54 By similarity. Interacts with KBTBD10. Ref.8

Subcellular location

Cytoplasmcell cortex By similarity. Cytoplasmcytoskeleton By similarity. Note: Associated with the F-actin rich cortical cytoskeleton By similarity.

Sequence similarities

Contains 1 LIM zinc-binding domain.

Contains 2 nebulin repeats.

Contains 1 SH3 domain.

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
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 261261LIM and SH3 domain protein 1
PRO_0000075761

Regions

Domain5 – 5652LIM zinc-binding
Repeat61 – 9535Nebulin 1
Repeat97 – 13135Nebulin 2
Domain202 – 26160SH3
Compositional bias201 – 2044Poly-Gly

Amino acid modifications

Modified residue11N-acetylmethionine Ref.3
Modified residue421N6-acetyllysine Ref.10
Modified residue681Phosphothreonine Ref.7 Ref.9 Ref.11
Modified residue1041Phosphothreonine Ref.5 Ref.7 Ref.9 Ref.11
Modified residue1121N6-succinyllysine By similarity
Modified residue1181Phosphoserine Ref.11
Modified residue1461Phosphoserine Ref.6 Ref.7 Ref.11

Natural variations

Alternative sequence201 – 26161GGGGK…YVEAI → ICLQHIPRHRIRPGRDPSIL QCLCFLKPATACDSYPSSSF FCQLKPSSATSAGSLLWQAS PLIDFLVFSLDGTGMGLSGG GRGPWGRAGMGDLLACGPHL PLCSLPSHPPAQLLTYPHIP GLG in isoform 2.
VSP_016554

Experimental info

Sequence conflict791E → R in AAH12460. Ref.2
Sequence conflict2101V → A in AAH12460. Ref.2
Sequence conflict2201E → A in AAH12460. Ref.2

Secondary structure

........... 261
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1998. Version 2.
Checksum: 3B89B988605B3639

FASTA26129,717
        10         20         30         40         50         60 
MNPNCARCGK IVYPTEKVNC LDKFWHKACF HCETCKMTLN MKNYKGYEKK PYCNAHYPKQ 

        70         80         90        100        110        120 
SFTMVADTPE NLRLKQQSEL QSQVRYKEEF EKNKGKGFSV VADTPELQRI KKTQDQISNI 

       130        140        150        160        170        180 
KYHEEFEKSR MGPSGGEGME PERRDSQDGS SYRRPLEQQQ PHHIPTSAPV YQQPQQQPVA 

       190        200        210        220        230        240 
QSYGGYKEPA APVSIQRSAP GGGGKRYRAV YDYSAADEDE VSFQDGDTIV NVQQIDDGWM 

       250        260 
YGTVERTGDT GMLPANYVEA I 

« Hide

Isoform 2 [UniParc].

Checksum: B6A28D1D97AB2C69
Show »

FASTA32336,014

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: DOMAINS.
[5]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[7]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68; THR-104 AND SER-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Novel beta-propeller of the BTB-Kelch protein Krp1 provides a binding site for Lasp-1 that is necessary for pseudopodial extension."
Gray C.H., McGarry L.C., Spence H.J., Riboldi-Tunnicliffe A., Ozanne B.W.
J. Biol. Chem. 284:30498-30507(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KBTBD10.
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68 AND THR-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68; THR-104; SER-118 AND SER-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X82456 mRNA. Translation: CAA57833.1.
BC007560 mRNA. Translation: AAH07560.1.
BC012460 mRNA. Translation: AAH12460.1.
PIRS68234.
RefSeqNP_001258537.1. NM_001271608.1.
NP_006139.1. NM_006148.3.
UniGeneHs.741156.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3I35X-ray1.40A202-261[»]
ProteinModelPortalQ14847.
SMRQ14847. Positions 1-54, 205-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110120. 17 interactions.
IntActQ14847. 14 interactions.
MINTMINT-5001286.
STRING9606.ENSP00000325240.

PTM databases

PhosphoSiteQ14847.

Polymorphism databases

DMDM3122342.

2D gel databases

OGPQ14847.
SWISS-2DPAGEQ14847.

Proteomic databases

PaxDbQ14847.
PRIDEQ14847.

Protocols and materials databases

DNASU3927.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318008; ENSP00000325240; ENSG00000002834. [Q14847-1]
ENST00000435347; ENSP00000392853; ENSG00000002834. [Q14847-1]
GeneID3927.
KEGGhsa:3927.
UCSCuc002hra.3. human. [Q14847-1]

Organism-specific databases

CTD3927.
GeneCardsGC17P037026.
HGNCHGNC:6513. LASP1.
HPACAB022049.
HPA012072.
MIM602920. gene.
neXtProtNX_Q14847.
PharmGKBPA30298.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG259964.
HOGENOMHOG000006616.
HOVERGENHBG054636.
InParanoidQ14847.
OMAYWHKACF.
OrthoDBEOG771280.
PhylomeDBQ14847.
TreeFamTF319104.

Gene expression databases

ArrayExpressQ14847.
BgeeQ14847.
CleanExHS_LASP1.
GenevestigatorQ14847.

Family and domain databases

Gene3D2.10.110.10. 1 hit.
InterProIPR000900. Nebulin_repeat.
IPR001452. SH3_domain.
IPR001781. Znf_LIM.
[Graphical view]
PfamPF00412. LIM. 1 hit.
PF00880. Nebulin. 2 hits.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00132. LIM. 1 hit.
SM00227. NEBU. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
PS51216. NEBULIN. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLASP1. human.
EvolutionaryTraceQ14847.
GeneWikiLASP1.
GenomeRNAi3927.
NextBio15423.
PROQ14847.
SOURCESearch...

Entry information

Entry nameLASP1_HUMAN
AccessionPrimary (citable) accession number: Q14847
Secondary accession number(s): Q96ED2, Q96IG0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM