Reviewed, UniProtKB/Swiss-Prot Q14847 (LASP1_HUMAN)

Names and origin

Protein names

Recommended name:
    LIM and SH3 domain protein 1
      Short name=LASP-1
Alternative name(s):
    MLN 50

Gene names

Name:	LASP1
Synonyms:	MLN50

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 binding Inferred from electronic annotation. Source: UniProtKB-KW ion transmembrane transporter activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred 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

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 1, 1998. Version 2. Checksum: 3B89B988605B3639	FASTA	261	29,717
	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
	Isoform 2 [UniParc]. Checksum: B6A28D1D97AB2C69		323	36,014
	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 ICLQHIPRHR IRPGRDPSIL QCLCFLKPAT ACDSYPSSSF 250 260 270 280 290 300 FCQLKPSSAT SAGSLLWQAS PLIDFLVFSL DGTGMGLSGG GRGPWGRAGM GDLLACGPHL 310 320 PLCSLPSHPP AQLLTYPHIP GLG

References

	« Hide 'large scale' referencesShow '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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBLGenBankDDBJ	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

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	November 25, 2008
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)