Q14847 (LASP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
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. Interacts with ANKRD54 By similarity. Interacts with KBTBD10. Ref.8
Subcellular location	Cytoplasm › cell cortex By similarity. Cytoplasm › cytoskeleton 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.

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	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	cortical actin cytoskeleton Inferred from sequence or structural similarity. Source: UniProtKB focal adhesion Inferred from electronic annotation. Source: Compara
Molecular_function	SH3/SH2 adaptor activity Traceable author statement Ref.4. Source: ProtInc ion transmembrane transporter activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MDFI	Q99750	3	EBI-742828,EBI-724076
TRIP13	Q15645	3	EBI-742828,EBI-358993

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 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 Ref.3

Modified residue

42

1

N6-acetyllysine Ref.10

Modified residue

68

1

Phosphothreonine Ref.7 Ref.9 Ref.11

Modified residue

104

1

Phosphothreonine Ref.5 Ref.7 Ref.9 Ref.11

Modified residue

118

1

Phosphoserine Ref.11

Modified residue

146

1

Phosphoserine Ref.6 Ref.7 Ref.11

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

261

Helix Strand Turn

Details...

Beta strand

207 – 211

5

Beta strand

228 – 236

9

Beta strand

239 – 244

6

Turn

245 – 248

4

Beta strand

249 – 254

6

Helix

255 – 257

3

Beta strand

258 – 260

3

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	FASTA	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] [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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X82456 mRNA. Translation: CAA57833.1.
BC007560 mRNA. Translation: AAH07560.1.
BC012460 mRNA. Translation: AAH12460.1.

IPI

IPI00000861.
IPI00386803.

PIR

S68234.

RefSeq

NP_001258537.1. NM_001271608.1.
NP_006139.1. NM_006148.3.

UniGene

Hs.741156.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3I35	X-ray	1.40	A	202-261	[»]

ProteinModelPortal

Q14847.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14847. 8 interactions.

MINT

MINT-5001286.

STRING

9606.ENSP00000325240.

PTM databases

PhosphoSite

Q14847.

Polymorphism databases

DMDM

3122342.

2D gel databases

OGP

Q14847.

SWISS-2DPAGE

Q14847.

Proteomic databases

PaxDb

Q14847.

PRIDE

Q14847.

Protocols and materials databases

DNASU

3927.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000318008; ENSP00000325240; ENSG00000002834.
ENST00000435347; ENSP00000392853; ENSG00000002834.

GeneID

3927.

KEGG

hsa:3927.

UCSC

uc002hra.3. human.

Organism-specific databases

CTD

3927.

GeneCards

GC17P037026.

HGNC

HGNC:6513. LASP1.

HPA

CAB022049.
HPA012072.

MIM

602920. gene.

neXtProt

NX_Q14847.

PharmGKB

PA30298.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG259964.

HOGENOM

HOG000006616.

HOVERGEN

HBG054636.

InParanoid

Q14847.

OMA

YWHKACF.

OrthoDB

EOG4PVP0H.

Gene expression databases

ArrayExpress

Q14847.

Bgee

Q14847.

CleanEx

HS_LASP1.

Genevestigator

Q14847.

GermOnline

ENSG00000002834. Homo sapiens.

Family and domain databases

Gene3D

2.10.110.10. 1 hit.

InterPro

IPR000900. Nebulin_35r-motif.
IPR001452. SH3_domain.
IPR001781. Znf_LIM.
[Graphical view]

Pfam

PF00412. LIM. 1 hit.
PF00880. Nebulin. 2 hits.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00452. SH3DOMAIN.

SMART

SM00132. LIM. 1 hit.
SM00227. NEBU. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

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

ChiTaRS

LASP1. human.

EvolutionaryTrace

Q14847.

GenomeRNAi

3927.

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:	May 1, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.