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Protein

LIM and SH3 domain protein 1

Gene

Lasp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  • actin filament binding Source: MGI
  • ion transmembrane transporter activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Actin-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
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 namesi
Name:Lasp1
Synonyms:Mln50
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:109656. Lasp1.

Subcellular locationi

GO - Cellular componenti

  • cortical actin cytoskeleton Source: UniProtKB
  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • focal adhesion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263LIM and SH3 domain protein 1PRO_0000075762Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei42 – 421N6-acetyllysineBy similarity
Modified residuei68 – 681PhosphothreonineBy similarity
Modified residuei104 – 1041PhosphothreonineCombined sources
Modified residuei112 – 1121N6-succinyllysineCombined sources
Modified residuei118 – 1181PhosphoserineBy similarity
Modified residuei156 – 1561Phosphothreonine; by PKA1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ61792.
MaxQBiQ61792.
PaxDbiQ61792.
PRIDEiQ61792.

PTM databases

iPTMnetiQ61792.
PhosphoSiteiQ61792.
SwissPalmiQ61792.

Expressioni

Gene expression databases

BgeeiQ61792.
CleanExiMM_LASP1.
ExpressionAtlasiQ61792. baseline and differential.
GenevisibleiQ61792. MM.

Interactioni

Subunit structurei

Interacts with F-actin. Interacts with KBTBD10 (By similarity). Interacts with ANKRD54.By similarity1 Publication

GO - Molecular functioni

  • actin filament binding Source: MGI

Protein-protein interaction databases

BioGridi201111. 7 interactions.
IntActiQ61792. 3 interactions.
MINTiMINT-1862350.
STRINGi10090.ENSMUSP00000042123.

Structurei

3D structure databases

ProteinModelPortaliQ61792.
SMRiQ61792. Positions 1-54, 207-263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 5652LIM zinc-bindingPROSITE-ProRule annotationAdd
BLAST
Repeati61 – 9535Nebulin 1Add
BLAST
Repeati97 – 13135Nebulin 2Add
BLAST
Domaini204 – 26360SH3PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi174 – 1807Poly-Gln
Compositional biasi203 – 2064Poly-Gly

Sequence similaritiesi

Contains 1 LIM zinc-binding domain.PROSITE-ProRule annotation
Contains 2 nebulin repeats.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat, SH3 domain

Phylogenomic databases

eggNOGiKOG1702. Eukaryota.
ENOG4111GQ8. LUCA.
GeneTreeiENSGT00530000062924.
HOGENOMiHOG000006616.
HOVERGENiHBG054636.
InParanoidiQ61792.
OMAiYGYKEPA.
PhylomeDBiQ61792.
TreeFamiTF319104.

Family and domain databases

Gene3Di2.10.110.10. 1 hit.
InterProiIPR000900. Nebulin_repeat.
IPR001452. SH3_domain.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 1 hit.
PF00880. Nebulin. 2 hits.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00132. LIM. 1 hit.
SM00227. NEBU. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
PS51216. NEBULIN. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q61792-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPNCARCGK IVYPTEKVNC LDKYWHKACF HCETCKMTLN MKNYKGYEKK
60 70 80 90 100
PYCNAHYPKQ SFTMVADTPE NLRLKQQSEL QSQVRYKEEF EKNKGKGFSV
110 120 130 140 150
VADTPELQRI KKTQDQISNI KYHEEFEKSR MGPSGGEGVE PERREAQDSS
160 170 180 190 200
SYRRPTEQQQ PQPHHIPTSA PVYQQPQQQQ MTSSYGGYKE PAAPVSIQRS
210 220 230 240 250
APGGGGKRYR AVYDYSAADE DEVSFQDGDT IVNVQQIDDG WMYGTVERTG
260
DTGMLPANYV EAI
Length:263
Mass (Da):29,994
Last modified:November 1, 1996 - v1
Checksum:iA6CA2FC2E451433E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96973 mRNA. Translation: CAA65659.1.
AK078445 mRNA. Translation: BAC37278.1.
BC010840 mRNA. Translation: AAH10840.1.
U58882 mRNA. Translation: AAC52639.1.
CCDSiCCDS25332.1.
RefSeqiNP_034818.1. NM_010688.4.
XP_006532404.1. XM_006532341.1.
UniGeneiMm.271967.
Mm.470698.

Genome annotation databases

EnsembliENSMUST00000043843; ENSMUSP00000042123; ENSMUSG00000038366.
GeneIDi16796.
KEGGimmu:16796.
UCSCiuc007lew.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96973 mRNA. Translation: CAA65659.1.
AK078445 mRNA. Translation: BAC37278.1.
BC010840 mRNA. Translation: AAH10840.1.
U58882 mRNA. Translation: AAC52639.1.
CCDSiCCDS25332.1.
RefSeqiNP_034818.1. NM_010688.4.
XP_006532404.1. XM_006532341.1.
UniGeneiMm.271967.
Mm.470698.

3D structure databases

ProteinModelPortaliQ61792.
SMRiQ61792. Positions 1-54, 207-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201111. 7 interactions.
IntActiQ61792. 3 interactions.
MINTiMINT-1862350.
STRINGi10090.ENSMUSP00000042123.

PTM databases

iPTMnetiQ61792.
PhosphoSiteiQ61792.
SwissPalmiQ61792.

Proteomic databases

EPDiQ61792.
MaxQBiQ61792.
PaxDbiQ61792.
PRIDEiQ61792.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043843; ENSMUSP00000042123; ENSMUSG00000038366.
GeneIDi16796.
KEGGimmu:16796.
UCSCiuc007lew.1. mouse.

Organism-specific databases

CTDi3927.
MGIiMGI:109656. Lasp1.

Phylogenomic databases

eggNOGiKOG1702. Eukaryota.
ENOG4111GQ8. LUCA.
GeneTreeiENSGT00530000062924.
HOGENOMiHOG000006616.
HOVERGENiHBG054636.
InParanoidiQ61792.
OMAiYGYKEPA.
PhylomeDBiQ61792.
TreeFamiTF319104.

Miscellaneous databases

ChiTaRSiLasp1. mouse.
NextBioi290666.
PROiQ61792.
SOURCEiSearch...

Gene expression databases

BgeeiQ61792.
CleanExiMM_LASP1.
ExpressionAtlasiQ61792. baseline and differential.
GenevisibleiQ61792. MM.

Family and domain databases

Gene3Di2.10.110.10. 1 hit.
InterProiIPR000900. Nebulin_repeat.
IPR001452. SH3_domain.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 1 hit.
PF00880. Nebulin. 2 hits.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00132. LIM. 1 hit.
SM00227. NEBU. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
PS51216. NEBULIN. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Chromosomal assignment and expression pattern of the murine Lasp-1 gene."
    Schreiber V., Masson R., Linares J.L., Mattei M.-G., Tomasetto C., Rio M.-C.
    Gene 207:171-175(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  3. "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].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  4. "Cloning of ligand targets: systematic isolation of SH3 domain-containing proteins."
    Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.
    Nat. Biotechnol. 14:741-744(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-263.
  5. "Phosphorylation of mouse LASP-1 on threonine 156 by cAMP- and cGMP-dependent protein kinase."
    Keicher C., Gambaryan S., Schulze E., Marcus K., Meyer H.E., Butt E.
    Biochem. Biophys. Res. Commun. 324:308-316(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-156.
  6. "Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that influences erythropoietin-induced differentiation."
    Samuels A.L., Klinken S.P., Ingley E.
    Blood 113:3845-3856(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANKRD54.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiLASP1_MOUSE
AccessioniPrimary (citable) accession number: Q61792
Secondary accession number(s): Q62416
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: March 16, 2016
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.